Alteration of V-type H+-ATPase during methyljasmonate-induced senescence in barley ( Hordeum vulgare L. cv. Salome)
Identifieur interne : 000749 ( Istex/Corpus ); précédent : 000748; suivant : 000750Alteration of V-type H+-ATPase during methyljasmonate-induced senescence in barley ( Hordeum vulgare L. cv. Salome)
Auteurs : R. Ratajczak ; I. Feussner ; B. Hause ; A. Böhm ; B. Parthier ; C. WasternackSource :
- Journal of Plant Physiology [ 0176-1617 ] ; 1998.
English descriptors
- KwdEn :
Abstract
In barley leaves, the application of (−)-jasmonic acid or its methyl ester (JAME) induces a senescencelike phenotype. This is accompanied by the synthesis of abundant proteins, so-called jasmonate-induced proteins (JlPs). Here, we show that modifications of vacuolar H+-ATPase (V-ATPase) subunits are jasmo-nate inducible. Using immunofluorescence analysis, we demonstrate that V-ATPase of barley leaves is exclusively located at the tonoplast also upon JAME treatment. Total ATP-hydrolysis activity of microsomal fractions increased by a factor of 10 during 72 h of JAME-treatment, while Bafilomycin Ai-sensitive ATP-hydrolysis activity, which is usually referred to V-ATPase activity, increased by a factor of about 2 in tono-plast-enriched membrane fractions. Moreover, due to JAME treatment there was a pronounced increase in ATP-hydrolysis activity at pH 6.2. This activity was not affected by inhibitors of P-, F-, or V-ATPases. However, biochemical analysis of partially purified V-ATPase suggests, that this activity might be due at least in part to the V-ATPase. JAME-treatment seems to change biochemical properties of the V-ATPase, i.e. a shift of the pH optimum of activity to a more acidic pH and a decrease in Bafilomycin A1 sensitivity. This is accompanied by the appearance of several additional forms of V-ATPase subunits which might represent either different isoforms or post-translationally modified proteins. We suggest that these changes in properties of the V-ATPase, which is involved in house-keeping and stress responses, may be due to JAME-induced senescence to overcome concomitant changes of the vacuolar membrane.
Url:
DOI: 10.1016/S0176-1617(98)80133-8
Links to Exploration step
ISTEX:AA2F4CB65804434D1086F7A002E03B9C18400E28Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Alteration of V-type H+-ATPase during methyljasmonate-induced senescence in barley ( Hordeum vulgare L. cv. Salome)</title><author><name sortKey="Ratajczak, R" sort="Ratajczak, R" uniqKey="Ratajczak R" first="R." last="Ratajczak">R. Ratajczak</name><affiliation><mods:affiliation>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</mods:affiliation></affiliation></author><author><name sortKey="Feussner, I" sort="Feussner, I" uniqKey="Feussner I" first="I." last="Feussner">I. Feussner</name><affiliation><mods:affiliation>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</mods:affiliation></affiliation></author><author><name sortKey="Hause, B" sort="Hause, B" uniqKey="Hause B" first="B." last="Hause">B. Hause</name><affiliation><mods:affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</mods:affiliation></affiliation></author><author><name sortKey="Bohm, A" sort="Bohm, A" uniqKey="Bohm A" first="A." last="Böhm">A. Böhm</name><affiliation><mods:affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</mods:affiliation></affiliation></author><author><name sortKey="Parthier, B" sort="Parthier, B" uniqKey="Parthier B" first="B." last="Parthier">B. Parthier</name><affiliation><mods:affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</mods:affiliation></affiliation></author><author><name sortKey="Wasternack, C" sort="Wasternack, C" uniqKey="Wasternack C" first="C." last="Wasternack">C. Wasternack</name><affiliation><mods:affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence.</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:AA2F4CB65804434D1086F7A002E03B9C18400E28</idno><date when="1998" year="1998">1998</date><idno type="doi">10.1016/S0176-1617(98)80133-8</idno><idno type="url">https://api.istex.fr/document/AA2F4CB65804434D1086F7A002E03B9C18400E28/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000749</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Alteration of V-type H+-ATPase during methyljasmonate-induced senescence in barley ( Hordeum vulgare L. cv. Salome)</title><author><name sortKey="Ratajczak, R" sort="Ratajczak, R" uniqKey="Ratajczak R" first="R." last="Ratajczak">R. Ratajczak</name><affiliation><mods:affiliation>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</mods:affiliation></affiliation></author><author><name sortKey="Feussner, I" sort="Feussner, I" uniqKey="Feussner I" first="I." last="Feussner">I. Feussner</name><affiliation><mods:affiliation>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</mods:affiliation></affiliation></author><author><name sortKey="Hause, B" sort="Hause, B" uniqKey="Hause B" first="B." last="Hause">B. Hause</name><affiliation><mods:affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</mods:affiliation></affiliation></author><author><name sortKey="Bohm, A" sort="Bohm, A" uniqKey="Bohm A" first="A." last="Böhm">A. Böhm</name><affiliation><mods:affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</mods:affiliation></affiliation></author><author><name sortKey="Parthier, B" sort="Parthier, B" uniqKey="Parthier B" first="B." last="Parthier">B. Parthier</name><affiliation><mods:affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</mods:affiliation></affiliation></author><author><name sortKey="Wasternack, C" sort="Wasternack, C" uniqKey="Wasternack C" first="C." last="Wasternack">C. Wasternack</name><affiliation><mods:affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Plant Physiology</title><title level="j" type="abbrev">JPLPH</title><idno type="ISSN">0176-1617</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">152</biblScope><biblScope unit="issue">2–3</biblScope><biblScope unit="page" from="199">199</biblScope><biblScope unit="page" to="206">206</biblScope></imprint><idno type="ISSN">0176-1617</idno></series><idno type="istex">AA2F4CB65804434D1086F7A002E03B9C18400E28</idno><idno type="DOI">10.1016/S0176-1617(98)80133-8</idno><idno type="PII">S0176-1617(98)80133-8</idno><idno type="ArticleID">80133</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0176-1617</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Altered subunits</term><term>BSA</term><term>DAPI</term><term>DTT</term><term>EDTA</term><term>FITC</term><term>HEPES</term><term>J1Ps</term><term>JAME</term><term>MES</term><term>PBS</term><term>PEG</term><term>SDS-PAGE</term><term>Tris</term><term>V-ATPase</term><term>biochemical properties</term><term>jasmonates</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract">In barley leaves, the application of (−)-jasmonic acid or its methyl ester (JAME) induces a senescencelike phenotype. This is accompanied by the synthesis of abundant proteins, so-called jasmonate-induced proteins (JlPs). Here, we show that modifications of vacuolar H+-ATPase (V-ATPase) subunits are jasmo-nate inducible. Using immunofluorescence analysis, we demonstrate that V-ATPase of barley leaves is exclusively located at the tonoplast also upon JAME treatment. Total ATP-hydrolysis activity of microsomal fractions increased by a factor of 10 during 72 h of JAME-treatment, while Bafilomycin Ai-sensitive ATP-hydrolysis activity, which is usually referred to V-ATPase activity, increased by a factor of about 2 in tono-plast-enriched membrane fractions. Moreover, due to JAME treatment there was a pronounced increase in ATP-hydrolysis activity at pH 6.2. This activity was not affected by inhibitors of P-, F-, or V-ATPases. However, biochemical analysis of partially purified V-ATPase suggests, that this activity might be due at least in part to the V-ATPase. JAME-treatment seems to change biochemical properties of the V-ATPase, i.e. a shift of the pH optimum of activity to a more acidic pH and a decrease in Bafilomycin A1 sensitivity. This is accompanied by the appearance of several additional forms of V-ATPase subunits which might represent either different isoforms or post-translationally modified proteins. We suggest that these changes in properties of the V-ATPase, which is involved in house-keeping and stress responses, may be due to JAME-induced senescence to overcome concomitant changes of the vacuolar membrane.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>R. Ratajczak</name><affiliations><json:string>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</json:string></affiliations></json:item><json:item><name>I. Feussner</name><affiliations><json:string>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</json:string></affiliations></json:item><json:item><name>B. Hause</name><affiliations><json:string>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</json:string></affiliations></json:item><json:item><name>A. Böhm</name><affiliations><json:string>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</json:string></affiliations></json:item><json:item><name>B. Parthier</name><affiliations><json:string>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</json:string></affiliations></json:item><json:item><name>C. Wasternack</name><affiliations><json:string>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</json:string><json:string>Correspondence.</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Altered subunits</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>biochemical properties</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>jasmonates</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>V-ATPase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>BSA : Bovine serum albumin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DAPI : 4,6-Diamidino-2-phenylindole</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DTT : Dithiothreitol</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>EDTA : Ethylendiaminetetraacetic acid</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>FITC : Fluorescein-5-isothiocyanate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>HEPES : N-(2-Hydroxyethyl)piperazine-N′-(2-ethanesulfonic acid)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>JAME : Jasmonic acid methylester</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>J1Ps : Jasmonate-induced proteins</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>MES : 2-(N-Morpholino)ethanesulfonic acid</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PBS : Phosphate buffered saline</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PEG : polyethylene glycol</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>SDS-PAGE : Sodium dodecyl sulphate-polyacrylamide gel electrophoresis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Tris : Tris(hydroxymethyl)aminomethane</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>V-ATPase : Vacuolar-type H+-ATPase</value></json:item></subject><articleId><json:string>80133</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>In barley leaves, the application of (−)-jasmonic acid or its methyl ester (JAME) induces a senescencelike phenotype. This is accompanied by the synthesis of abundant proteins, so-called jasmonate-induced proteins (JlPs). Here, we show that modifications of vacuolar H+-ATPase (V-ATPase) subunits are jasmo-nate inducible. Using immunofluorescence analysis, we demonstrate that V-ATPase of barley leaves is exclusively located at the tonoplast also upon JAME treatment. Total ATP-hydrolysis activity of microsomal fractions increased by a factor of 10 during 72 h of JAME-treatment, while Bafilomycin Ai-sensitive ATP-hydrolysis activity, which is usually referred to V-ATPase activity, increased by a factor of about 2 in tono-plast-enriched membrane fractions. Moreover, due to JAME treatment there was a pronounced increase in ATP-hydrolysis activity at pH 6.2. This activity was not affected by inhibitors of P-, F-, or V-ATPases. However, biochemical analysis of partially purified V-ATPase suggests, that this activity might be due at least in part to the V-ATPase. JAME-treatment seems to change biochemical properties of the V-ATPase, i.e. a shift of the pH optimum of activity to a more acidic pH and a decrease in Bafilomycin A1 sensitivity. This is accompanied by the appearance of several additional forms of V-ATPase subunits which might represent either different isoforms or post-translationally modified proteins. We suggest that these changes in properties of the V-ATPase, which is involved in house-keeping and stress responses, may be due to JAME-induced senescence to overcome concomitant changes of the vacuolar membrane.</abstract><qualityIndicators><score>9.698</score><pdfVersion>1.7</pdfVersion><pdfPageSize>576 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>18</keywordCount><abstractCharCount>1643</abstractCharCount><pdfWordCount>4854</pdfWordCount><pdfCharCount>30673</pdfCharCount><pdfPageCount>8</pdfPageCount><abstractWordCount>237</abstractWordCount></qualityIndicators><title>Alteration of V-type H+-ATPase during methyljasmonate-induced senescence in barley ( Hordeum vulgare L. cv. Salome)</title><pii><json:string>S0176-1617(98)80133-8</json:string></pii><genre><json:string>research-article</json:string></genre><host><volume>152</volume><pii><json:string>S0176-1617(98)X8122-8</json:string></pii><pages><last>206</last><first>199</first></pages><issn><json:string>0176-1617</json:string></issn><issue>2–3</issue><genre><json:string>journal</json:string></genre><language><json:string>unknown</json:string></language><title>Journal of Plant Physiology</title><publicationDate>1998</publicationDate></host><categories><wos><json:string>PLANT SCIENCES</json:string></wos></categories><publicationDate>1998</publicationDate><copyrightDate>1998</copyrightDate><doi><json:string>10.1016/S0176-1617(98)80133-8</json:string></doi><id>AA2F4CB65804434D1086F7A002E03B9C18400E28</id><score>0.3089112</score><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/AA2F4CB65804434D1086F7A002E03B9C18400E28/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/AA2F4CB65804434D1086F7A002E03B9C18400E28/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/AA2F4CB65804434D1086F7A002E03B9C18400E28/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Alteration of V-type H+-ATPase during methyljasmonate-induced senescence in barley ( Hordeum vulgare L. cv. Salome)</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>©1998 Gustav Fischer Verlag, Jena</p></availability><date>1998</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Alteration of V-type H+-ATPase during methyljasmonate-induced senescence in barley ( Hordeum vulgare L. cv. Salome)</title><author xml:id="author-1"><persName><forename type="first">R.</forename><surname>Ratajczak</surname></persName><affiliation>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</affiliation></author><author xml:id="author-2"><persName><forename type="first">I.</forename><surname>Feussner</surname></persName><affiliation>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</affiliation></author><author xml:id="author-3"><persName><forename type="first">B.</forename><surname>Hause</surname></persName><affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</affiliation></author><author xml:id="author-4"><persName><forename type="first">A.</forename><surname>Böhm</surname></persName><affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</affiliation></author><author xml:id="author-5"><persName><forename type="first">B.</forename><surname>Parthier</surname></persName><affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</affiliation></author><author xml:id="author-6"><persName><forename type="first">C.</forename><surname>Wasternack</surname></persName><affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</affiliation><affiliation>Correspondence.</affiliation></author></analytic><monogr><title level="j">Journal of Plant Physiology</title><title level="j" type="abbrev">JPLPH</title><idno type="pISSN">0176-1617</idno><idno type="PII">S0176-1617(98)X8122-8</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998"></date><biblScope unit="volume">152</biblScope><biblScope unit="issue">2–3</biblScope><biblScope unit="page" from="199">199</biblScope><biblScope unit="page" to="206">206</biblScope></imprint></monogr><idno type="istex">AA2F4CB65804434D1086F7A002E03B9C18400E28</idno><idno type="DOI">10.1016/S0176-1617(98)80133-8</idno><idno type="PII">S0176-1617(98)80133-8</idno><idno type="ArticleID">80133</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1998</date></creation><langUsage><language ident="en">en</language></langUsage><abstract><p>In barley leaves, the application of (−)-jasmonic acid or its methyl ester (JAME) induces a senescencelike phenotype. This is accompanied by the synthesis of abundant proteins, so-called jasmonate-induced proteins (JlPs). Here, we show that modifications of vacuolar H+-ATPase (V-ATPase) subunits are jasmo-nate inducible. Using immunofluorescence analysis, we demonstrate that V-ATPase of barley leaves is exclusively located at the tonoplast also upon JAME treatment. Total ATP-hydrolysis activity of microsomal fractions increased by a factor of 10 during 72 h of JAME-treatment, while Bafilomycin Ai-sensitive ATP-hydrolysis activity, which is usually referred to V-ATPase activity, increased by a factor of about 2 in tono-plast-enriched membrane fractions. Moreover, due to JAME treatment there was a pronounced increase in ATP-hydrolysis activity at pH 6.2. This activity was not affected by inhibitors of P-, F-, or V-ATPases. However, biochemical analysis of partially purified V-ATPase suggests, that this activity might be due at least in part to the V-ATPase. JAME-treatment seems to change biochemical properties of the V-ATPase, i.e. a shift of the pH optimum of activity to a more acidic pH and a decrease in Bafilomycin A1 sensitivity. This is accompanied by the appearance of several additional forms of V-ATPase subunits which might represent either different isoforms or post-translationally modified proteins. We suggest that these changes in properties of the V-ATPase, which is involved in house-keeping and stress responses, may be due to JAME-induced senescence to overcome concomitant changes of the vacuolar membrane.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Key words</head><item><term>Altered subunits</term></item><item><term>biochemical properties</term></item><item><term>jasmonates</term></item><item><term>V-ATPase</term></item></list></keywords></textClass><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>BSA</term><term>Bovine serum albumin</term></item><item><term>DAPI</term><term>4,6-Diamidino-2-phenylindole</term></item><item><term>DTT</term><term>Dithiothreitol</term></item><item><term>EDTA</term><term>Ethylendiaminetetraacetic acid</term></item><item><term>FITC</term><term>Fluorescein-5-isothiocyanate</term></item><item><term>HEPES</term><term>N-(2-Hydroxyethyl)piperazine-N′-(2-ethanesulfonic acid)</term></item><item><term>JAME</term><term>Jasmonic acid methylester</term></item><item><term>J1Ps</term><term>Jasmonate-induced proteins</term></item><item><term>MES</term><term>2-(N-Morpholino)ethanesulfonic acid</term></item><item><term>PBS</term><term>Phosphate buffered saline</term></item><item><term>PEG</term><term>polyethylene glycol</term></item><item><term>SDS-PAGE</term><term>Sodium dodecyl sulphate-polyacrylamide gel electrophoresis</term></item><item><term>Tris</term><term>Tris(hydroxymethyl)aminomethane</term></item><item><term>V-ATPase</term><term>Vacuolar-type H+-ATPase</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/AA2F4CB65804434D1086F7A002E03B9C18400E28/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier doc found" wicri:toSee="Elsevier, no converted or simple article"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" </istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 5.1.0//EN//XML" URI="art510.dtd" name="istex:docType"></istex:docType><istex:document><article version="5.1" xml:lang="en" docsubtype="fla"><item-info><jid>JPLPH</jid><aid>80133</aid><ce:pii>S0176-1617(98)80133-8</ce:pii><ce:doi>10.1016/S0176-1617(98)80133-8</ce:doi><ce:copyright type="other" year="1998">Gustav Fischer Verlag, Jena</ce:copyright></item-info><head><ce:title>Alteration of V-type H<ce:sup>+</ce:sup>-ATPase during methyljasmonate-induced senescence in barley (<ce:italic>Hordeum vulgare</ce:italic> L. cv. Salome)</ce:title><ce:dedication>This report is dedicated to Prof. Dr. Martin Bopp, Heidelberg, on the occasion of his 75th birthday.</ce:dedication><ce:author-group><ce:author><ce:given-name>R.</ce:given-name><ce:surname>Ratajczak</ce:surname><ce:cross-ref refid="aff1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>I.</ce:given-name><ce:surname>Feussner</ce:surname><ce:cross-ref refid="aff1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>B.</ce:given-name><ce:surname>Hause</ce:surname><ce:cross-ref refid="aff2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>A.</ce:given-name><ce:surname>Böhm</ce:surname><ce:cross-ref refid="aff2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>B.</ce:given-name><ce:surname>Parthier</ce:surname><ce:cross-ref refid="aff2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>C.</ce:given-name><ce:surname>Wasternack</ce:surname><ce:cross-ref refid="aff2"><ce:sup>2</ce:sup></ce:cross-ref><ce:cross-ref refid="cor1"><ce:sup>*</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="aff1"><ce:label>1</ce:label><ce:textfn>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</ce:textfn></ce:affiliation><ce:affiliation id="aff2"><ce:label>2</ce:label><ce:textfn>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</ce:textfn></ce:affiliation><ce:correspondence id="cor1"><ce:label>*</ce:label><ce:text>Correspondence.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="1" month="9" year="1997"></ce:date-received><ce:date-accepted day="31" month="10" year="1997"></ce:date-accepted><ce:abstract id="ab1"><ce:section-title>Summary</ce:section-title><ce:abstract-sec><ce:simple-para id="SP0005">In barley leaves, the application of (−)-jasmonic acid or its methyl ester (JAME) induces a senescencelike phenotype. This is accompanied by the synthesis of abundant proteins, so-called jasmonate-induced proteins (JlPs). Here, we show that modifications of vacuolar H<ce:sup>+</ce:sup>-ATPase (V-ATPase) subunits are jasmo-nate inducible. Using immunofluorescence analysis, we demonstrate that V-ATPase of barley leaves is exclusively located at the tonoplast also upon JAME treatment. Total ATP-hydrolysis activity of microsomal fractions increased by a factor of 10 during 72 h of JAME-treatment, while Bafilomycin Ai-sensitive ATP-hydrolysis activity, which is usually referred to V-ATPase activity, increased by a factor of about 2 in tono-plast-enriched membrane fractions. Moreover, due to JAME treatment there was a pronounced increase in ATP-hydrolysis activity at pH 6.2. This activity was not affected by inhibitors of P-, F-, or V-ATPases. However, biochemical analysis of partially purified V-ATPase suggests, that this activity might be due at least in part to the V-ATPase. JAME-treatment seems to change biochemical properties of the V-ATPase, i.e. a shift of the pH optimum of activity to a more acidic pH and a decrease in Bafilomycin A1 sensitivity. This is accompanied by the appearance of several additional forms of V-ATPase subunits which might represent either different isoforms or post-translationally modified proteins. We suggest that these changes in properties of the V-ATPase, which is involved in house-keeping and stress responses, may be due to JAME-induced senescence to overcome concomitant changes of the vacuolar membrane.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword"><ce:section-title>Key words</ce:section-title><ce:keyword><ce:text>Altered subunits</ce:text></ce:keyword><ce:keyword><ce:text>biochemical properties</ce:text></ce:keyword><ce:keyword><ce:text>jasmonates</ce:text></ce:keyword><ce:keyword><ce:text>V-ATPase</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>BSA</ce:text><ce:keyword><ce:text>Bovine serum albumin</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>DAPI</ce:text><ce:keyword><ce:text>4,6-Diamidino-2-phenylindole</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>DTT</ce:text><ce:keyword><ce:text>Dithiothreitol</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>EDTA</ce:text><ce:keyword><ce:text>Ethylendiaminetetraacetic acid</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>FITC</ce:text><ce:keyword><ce:text>Fluorescein-5-isothiocyanate</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>HEPES</ce:text><ce:keyword><ce:text>N-(2-Hydroxyethyl)piperazine-N′-(2-ethanesulfonic acid)</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>JAME</ce:text><ce:keyword><ce:text>Jasmonic acid methylester</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>J1Ps</ce:text><ce:keyword><ce:text>Jasmonate-induced proteins</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>MES</ce:text><ce:keyword><ce:text>2-(N-Morpholino)ethanesulfonic acid</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>PBS</ce:text><ce:keyword><ce:text>Phosphate buffered saline</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>PEG</ce:text><ce:keyword><ce:text>polyethylene glycol</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>SDS-PAGE</ce:text><ce:keyword><ce:text>Sodium dodecyl sulphate-polyacrylamide gel electrophoresis</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>Tris</ce:text><ce:keyword><ce:text>Tris(hydroxymethyl)aminomethane</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>V-ATPase</ce:text><ce:keyword><ce:text>Vacuolar-type H<ce:sup>+</ce:sup>-ATPase</ce:text></ce:keyword></ce:keyword></ce:keywords></head><tail><ce:bibliography id="R0005"><ce:section-title>References</ce:section-title><ce:bibliography-sec id="RS0005"><ce:bib-reference id="bib1"><ce:label>Bañuls et al., 1995</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>J.</ce:given-name><ce:surname>Bañuls</ce:surname></sb:author><sb:author><ce:given-name>R.</ce:given-name><ce:surname>Ratajczak</ce:surname></sb:author><sb:author><ce:given-name>U.</ce:given-name><ce:surname>Lüttge</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>NaCl stress enhances proteolytic turnover of the tonoplast H<ce:sup>+</ce:sup>-ATPase of Citrus sinensis: appearance of a 35 kDa fragment of subunit A still exhibiting ATP-hydrolysis activity?</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Plant Cell Environ.</sb:maintitle></sb:title><sb:volume-nr>18</sb:volume-nr></sb:series><sb:date>1995</sb:date></sb:issue><sb:pages><sb:first-page>1341</sb:first-page><sb:last-page>1344</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib2"><ce:label>Becker and Apel, 1992</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>W.</ce:given-name><ce:surname>Becker</ce:surname></sb:author><sb:author><ce:given-name>K.</ce:given-name><ce:surname>Apel</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Isolation and characterization of a cDNA clone encoding a novel jasmonate-induced protein of barley (<ce:italic>Hordeum vulgare</ce:italic> L)</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Plant Mol. Biol.</sb:maintitle></sb:title><sb:volume-nr>19</sb:volume-nr></sb:series><sb:date>1992</sb:date></sb:issue><sb:pages><sb:first-page>1065</sb:first-page><sb:last-page>1067</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib3"><ce:label>Bremberger et al., 1988</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>C.</ce:given-name><ce:surname>Bremberger</ce:surname></sb:author><sb:author><ce:given-name>H.-P.</ce:given-name><ce:surname>Haschke</ce:surname></sb:author><sb:author><ce:given-name>U.</ce:given-name><ce:surname>Lüttge</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Separation and purification of the tonoplast ATPase and pyrophosphatase from plants with constitutive and inducible crassulacean acid metabolism</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Planta</sb:maintitle></sb:title><sb:volume-nr>175</sb:volume-nr></sb:series><sb:date>1988</sb:date></sb:issue><sb:pages><sb:first-page>465</sb:first-page><sb:last-page>470</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib4"><ce:label>Creelman and Mullet, 1997</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>R.A.</ce:given-name><ce:surname>Creelman</ce:surname></sb:author><sb:author><ce:given-name>J.E.</ce:given-name><ce:surname>Mullet</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Biosynthesis and action of jas-monates in plants</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Ann. Rev. Plant Physiol. Plant Mol. Biol.</sb:maintitle></sb:title><sb:volume-nr>48</sb:volume-nr></sb:series><sb:date>1997</sb:date></sb:issue><sb:pages><sb:first-page>355</sb:first-page><sb:last-page>381</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib5"><ce:label>Feussner et al., 1995</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>I.</ce:given-name><ce:surname>Feussner</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Hause</ce:surname></sb:author><sb:author><ce:given-name>K.</ce:given-name><ce:surname>Vörös</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Parthier</ce:surname></sb:author><sb:author><ce:given-name>C.</ce:given-name><ce:surname>Wasternack</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Jasmonate-induced lipoxygenase forms are localized in chloroplasts of barley leaves (<ce:italic>Hordeum vulgare</ce:italic> cv. Salome)</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Plant J.</sb:maintitle></sb:title><sb:volume-nr>7</sb:volume-nr></sb:series><sb:date>1995</sb:date></sb:issue><sb:pages><sb:first-page>949</sb:first-page><sb:last-page>957</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib6"><ce:label>Gallagher and Leonard, 1982</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>S.R.</ce:given-name><ce:surname>Gallagher</ce:surname></sb:author><sb:author><ce:given-name>R.T.</ce:given-name><ce:surname>Leonard</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Effect of vanadate, molyb-date, and azide on membrane-associated ATPase and soluble phosphatase activities of corn roots</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Plant Physiol.</sb:maintitle></sb:title><sb:volume-nr>70</sb:volume-nr></sb:series><sb:date>1982</sb:date></sb:issue><sb:pages><sb:first-page>1335</sb:first-page><sb:last-page>1340</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib7"><ce:label>Görschen et al., 1997</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>E.</ce:given-name><ce:surname>Görschen</ce:surname></sb:author><sb:author><ce:given-name>M.</ce:given-name><ce:surname>Dunaeva</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Hause</ce:surname></sb:author><sb:author><ce:given-name>I.</ce:given-name><ce:surname>Reeh</ce:surname></sb:author><sb:author><ce:given-name>C.</ce:given-name><ce:surname>Wasternack</ce:surname></sb:author><sb:author><ce:given-name>P.</ce:given-name><ce:surname>Parthier</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Expression of the ribosome-inactivating protein JIP60 from barley in transgenic tobacco leads to an abnormal phenotype and alterations on the level of translation</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Planta</sb:maintitle></sb:title><sb:volume-nr>202</sb:volume-nr></sb:series><sb:date>1997</sb:date></sb:issue><sb:pages><sb:first-page>470</sb:first-page><sb:last-page>478</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib8"><ce:label>Haschke et al., 1989</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>H.-P.</ce:given-name><ce:surname>Haschke</ce:surname></sb:author><sb:author><ce:given-name>C.</ce:given-name><ce:surname>Bremberger</ce:surname></sb:author><sb:author><ce:given-name>U.</ce:given-name><ce:surname>Lüttge</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Transport proteins in plants with crassulacean acid metabolism: immunological characterization of ATPase subunits</sb:maintitle></sb:title></sb:contribution><sb:host><sb:edited-book><sb:editors><sb:editor><ce:given-name>J.</ce:given-name><ce:surname>Dainty</ce:surname></sb:editor><sb:editor><ce:given-name>M.I.</ce:given-name><ce:surname>De Michelis</ce:surname></sb:editor><sb:editor><ce:given-name>E.</ce:given-name><ce:surname>Marre</ce:surname></sb:editor><sb:editor><ce:given-name>F.</ce:given-name><ce:surname>Rassi-Caldogno</ce:surname></sb:editor></sb:editors><sb:title><sb:maintitle>Plant membrane transport</sb:maintitle></sb:title><sb:date>1989</sb:date><sb:publisher><sb:name>Elsevier Science Publishers B.V.</sb:name><sb:location>Amsterdam</sb:location></sb:publisher></sb:edited-book><sb:pages><sb:first-page>149</sb:first-page><sb:last-page>154</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib9"><ce:label>Hause et al., 1994</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Hause</ce:surname></sb:author><sb:author><ce:given-name>U.</ce:given-name><ce:surname>zur Nieden</ce:surname></sb:author><sb:author><ce:given-name>J.</ce:given-name><ce:surname>Lehmann</ce:surname></sb:author><sb:author><ce:given-name>C.</ce:given-name><ce:surname>Wasternack</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Parthier</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Intracellular localization of jasmonate-induced proteins in barley leaves</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Bot. Acta</sb:maintitle></sb:title><sb:volume-nr>107</sb:volume-nr></sb:series><sb:date>1994</sb:date></sb:issue><sb:pages><sb:first-page>333</sb:first-page><sb:last-page>341</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib10"><ce:label>Hause et al., 1996</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Hause</ce:surname></sb:author><sb:author><ce:given-name>U.</ce:given-name><ce:surname>Demus</ce:surname></sb:author><sb:author><ce:given-name>C.</ce:given-name><ce:surname>Teichmann</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Parthier</ce:surname></sb:author><sb:author><ce:given-name>C.</ce:given-name><ce:surname>Wasternack</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Developmental and tissue-specific expression of JIP-23, a jasmonate-inducible protein of barley</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Plant Cell Physiol.</sb:maintitle></sb:title><sb:volume-nr>37</sb:volume-nr></sb:series><sb:date>1996</sb:date></sb:issue><sb:pages><sb:first-page>641</sb:first-page><sb:last-page>649</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib11"><ce:label>Kelly and Davis, 1988</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>M.O.</ce:given-name><ce:surname>Kelly</ce:surname></sb:author><sb:author><ce:given-name>P.J.</ce:given-name><ce:surname>Davis</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>The control of whole plant senescence</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>CRC Critical Reviews in Plant Science</sb:maintitle></sb:title><sb:volume-nr>7</sb:volume-nr></sb:series><sb:date>1988</sb:date></sb:issue><sb:pages><sb:first-page>139</sb:first-page><sb:last-page>173</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib12"><ce:label>Klink and Lüttge, 1992</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>R.</ce:given-name><ce:surname>Klink</ce:surname></sb:author><sb:author><ce:given-name>U.</ce:given-name><ce:surname>Lüttge</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Quantification of visible structural changes of the leaf-ATPase in the leaf-tonoplast of <ce:italic>Mesembryan-themum crystallinum</ce:italic> by freeze-fracture replicas prepared during the C-3-photosynthesis to CAM transition</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Bot. Acta</sb:maintitle></sb:title><sb:volume-nr>105</sb:volume-nr></sb:series><sb:date>1992</sb:date></sb:issue><sb:pages><sb:first-page>414</sb:first-page><sb:last-page>420</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib13"><ce:label>Leopold et al., 1996</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>J.</ce:given-name><ce:surname>Leopold</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Hause</ce:surname></sb:author><sb:author><ce:given-name>J.</ce:given-name><ce:surname>Lehmann</ce:surname></sb:author><sb:author><ce:given-name>A.</ce:given-name><ce:surname>Graner</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Parthier</ce:surname></sb:author><sb:author><ce:given-name>C.</ce:given-name><ce:surname>Wasternack</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Isolation, characterization and expression of a cDNA coding for a jasmonate-inducible protein of 37kDa in barley leaves</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Plant Cell Environ.</sb:maintitle></sb:title><sb:volume-nr>19</sb:volume-nr></sb:series><sb:date>1996</sb:date></sb:issue><sb:pages><sb:first-page>675</sb:first-page><sb:last-page>684</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib14"><ce:label>Lüttge and Ratajczak, 1997</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>U.</ce:given-name><ce:surname>Lüttge</ce:surname></sb:author><sb:author><ce:given-name>R.</ce:given-name><ce:surname>Ratajczak</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>The physiology, biochemistry and molecular biology of the plant vacuolar ATPase</sb:maintitle></sb:title></sb:contribution><sb:host><sb:edited-book><sb:editors><sb:editor><ce:given-name>R.</ce:given-name><ce:surname>Leigh</ce:surname></sb:editor><sb:editor><ce:given-name>D.</ce:given-name><ce:surname>Sanders</ce:surname></sb:editor></sb:editors><sb:title><sb:maintitle>Advances in Botanical Research, Vol. 25, The Plant Vacuole</sb:maintitle></sb:title><sb:date>1997</sb:date><sb:publisher><sb:name>Academic Press</sb:name><sb:location>Oxford</sb:location></sb:publisher></sb:edited-book><sb:pages><sb:first-page>253</sb:first-page><sb:last-page>296</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib15"><ce:label>Lüttge et al., 1995</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>U.</ce:given-name><ce:surname>Lüttge</ce:surname></sb:author><sb:author><ce:given-name>R.</ce:given-name><ce:surname>Ratajczak</ce:surname></sb:author><sb:author><ce:given-name>T.</ce:given-name><ce:surname>Rausch</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Rockel</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Stress responses of tonoplast proteins: an example for molecular ecophys-iology and the search for eco-enzymes</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Acta Bot. Neerl.</sb:maintitle></sb:title><sb:volume-nr>44</sb:volume-nr></sb:series><sb:date>1995</sb:date></sb:issue><sb:pages><sb:first-page>343</sb:first-page><sb:last-page>362</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib16"><ce:label>Narasimhan et al., 1991</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>M.L.</ce:given-name><ce:surname>Narasimhan</ce:surname></sb:author><sb:author><ce:given-name>M.L.</ce:given-name><ce:surname>Binzel</ce:surname></sb:author><sb:author><ce:given-name>E.</ce:given-name><ce:surname>Perez-Prat</ce:surname></sb:author><sb:author><ce:given-name>Z.</ce:given-name><ce:surname>Chen</ce:surname></sb:author><sb:author><ce:given-name>D.E.</ce:given-name><ce:surname>Nelson</ce:surname></sb:author><sb:author><ce:given-name>N.K.</ce:given-name><ce:surname>Singh</ce:surname></sb:author><sb:author><ce:given-name>R.A.</ce:given-name><ce:surname>Bressan</ce:surname></sb:author><sb:author><ce:given-name>P.M.</ce:given-name><ce:surname>Hasegawa</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>NaCl regulation of tonoplast ATPase 70-kilodalton subunit mRNA in tobacco cells</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Plant Physiol.</sb:maintitle></sb:title><sb:volume-nr>97</sb:volume-nr></sb:series><sb:date>1991</sb:date></sb:issue><sb:pages><sb:first-page>562</sb:first-page><sb:last-page>568</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib17"><ce:label>Nørby, 1988</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>J.G.</ce:given-name><ce:surname>Nørby</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Coupled assay of Na<ce:sup>+</ce:sup>, K<ce:sup>+</ce:sup>-ATPase activity</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Meth. Enzymology</sb:maintitle></sb:title><sb:volume-nr>156</sb:volume-nr></sb:series><sb:date>1988</sb:date></sb:issue><sb:pages><sb:first-page>116</sb:first-page><sb:last-page>119</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib18"><ce:label>Parthier, 1991</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Parthier</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Jasmonates, new regulators of plant growth and development, many facts and few hypotheses on their actions</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Bot. Acta</sb:maintitle></sb:title><sb:volume-nr>104</sb:volume-nr></sb:series><sb:date>1991</sb:date></sb:issue><sb:pages><sb:first-page>446</sb:first-page><sb:last-page>454</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib19"><ce:label>Ratajczak, 1994</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>R.</ce:given-name><ce:surname>Ratajczak</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>The non-ionic detergent Brij 58 conserves the structure of the tonoplast H<ce:sup>+</ce:sup>-ATPase of <ce:italic>Mesembryanthemum crystallinum</ce:italic> L. during solubilization and partial purification</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Bot. Acta</sb:maintitle></sb:title><sb:volume-nr>107</sb:volume-nr></sb:series><sb:date>1994</sb:date></sb:issue><sb:pages><sb:first-page>201</sb:first-page><sb:last-page>209</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib20"><ce:label>Ratajczak et al., 1995</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>R.</ce:given-name><ce:surname>Ratajczak</ce:surname></sb:author><sb:author><ce:given-name>A.</ce:given-name><ce:surname>Hille</ce:surname></sb:author><sb:author><ce:given-name>J.B.</ce:given-name><ce:surname>Mariaux</ce:surname></sb:author><sb:author><ce:given-name>U.</ce:given-name><ce:surname>Lüttge</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Quantitative stress responses of the V<ce:inf>0</ce:inf>V<ce:inf>1</ce:inf>-ATPase of higher plants detected by immune-electron microscopy</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Bot. Acta</sb:maintitle></sb:title><sb:volume-nr>108</sb:volume-nr></sb:series><sb:date>1995</sb:date></sb:issue><sb:pages><sb:first-page>505</sb:first-page><sb:last-page>513</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib21"><ce:label>Ratajczak et al., 1994</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>R.</ce:given-name><ce:surname>Ratajczak</ce:surname></sb:author><sb:author><ce:given-name>J.</ce:given-name><ce:surname>Richter</ce:surname></sb:author><sb:author><ce:given-name>U.</ce:given-name><ce:surname>Lüttge</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Adaptation of the tonoplast V-type H<ce:sup>+</ce:sup>-ATPase of <ce:italic>Mesembryanthemum crystallinum</ce:italic> to salt stress, C<ce:inf>3</ce:inf>-CAM transition and plant age</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Plant Cell Environm.</sb:maintitle></sb:title><sb:volume-nr>17</sb:volume-nr></sb:series><sb:date>1994</sb:date></sb:issue><sb:pages><sb:first-page>1101</sb:first-page><sb:last-page>1112</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib22"><ce:label>Reuveni et al., 1990</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>M.</ce:given-name><ce:surname>Reuveni</ce:surname></sb:author><sb:author><ce:given-name>A.B.</ce:given-name><ce:surname>Bennett</ce:surname></sb:author><sb:author><ce:given-name>R.A.</ce:given-name><ce:surname>Bressan</ce:surname></sb:author><sb:author><ce:given-name>P.M.</ce:given-name><ce:surname>Hasegawa</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Enhanced H<ce:sup>+</ce:sup>-transport capacity and ATP-hydrolysis activity of the tonoplast H<ce:sup>+</ce:sup>-ATPase after NaCl adaptation</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Plant Physiol.</sb:maintitle></sb:title><sb:volume-nr>94</sb:volume-nr></sb:series><sb:date>1990</sb:date></sb:issue><sb:pages><sb:first-page>524</sb:first-page><sb:last-page>530</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib23"><ce:label>Rockel et al., 1994</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Rockel</ce:surname></sb:author><sb:author><ce:given-name>R.</ce:given-name><ce:surname>Ratajczak</ce:surname></sb:author><sb:author><ce:given-name>A.</ce:given-name><ce:surname>Becker</ce:surname></sb:author><sb:author><ce:given-name>U.</ce:given-name><ce:surname>Lüttge</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Changed densities and diameters of intra-membrane tonoplast particles of <ce:italic>Mesembryanthemum crystallinum</ce:italic> in correlation with NaCl-induced CAM</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>J. Plant Physiol.</sb:maintitle></sb:title><sb:volume-nr>143</sb:volume-nr></sb:series><sb:date>1994</sb:date></sb:issue><sb:pages><sb:first-page>318</sb:first-page><sb:last-page>324</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib24"><ce:label>Sembdner and Parthier, 1993</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>G.</ce:given-name><ce:surname>Sembdner</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Parthier</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>The biochemistry and the physiological and molecular actions of jasmonates</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Annu. Rev. Plant Physiol. Plant Mol. Biol.</sb:maintitle></sb:title><sb:volume-nr>44</sb:volume-nr></sb:series><sb:date>1993</sb:date></sb:issue><sb:pages><sb:first-page>569</sb:first-page><sb:last-page>589</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib25"><ce:label>Thimann, 1987</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>K.V.</ce:given-name><ce:surname>Thimann</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Plant senescence: a proposed integration of the constituent processes</sb:maintitle></sb:title></sb:contribution><sb:host><sb:edited-book><sb:editors><sb:editor><ce:given-name>W.W.</ce:given-name><ce:surname>Thomson</ce:surname></sb:editor><sb:editor><ce:given-name>E.A.</ce:given-name><ce:surname>Nothnagel</ce:surname></sb:editor><sb:editor><ce:given-name>R.C.</ce:given-name><ce:surname>Huffaker</ce:surname></sb:editor></sb:editors><sb:title><sb:maintitle>Plant senescence: its biochemistry and physiology</sb:maintitle></sb:title><sb:date>1987</sb:date><sb:publisher><sb:name>The American Society of Plant Physiologists</sb:name><sb:location>Rockville, MD</sb:location></sb:publisher></sb:edited-book><sb:pages><sb:first-page>1</sb:first-page><sb:last-page>19</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib26"><ce:label>Van Lammeren et al., 1985</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>A.A.M.</ce:given-name><ce:surname>Van Lammeren</ce:surname></sb:author><sb:author><ce:given-name>C.J.</ce:given-name><ce:surname>Keijzer</ce:surname></sb:author><sb:author><ce:given-name>M.T.M.</ce:given-name><ce:surname>Willemse</ce:surname></sb:author><sb:author><ce:given-name>H.</ce:given-name><ce:surname>Kieft</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Structure and function of the microtubular cytoskele-ton during pollen development in <ce:italic>Gasteria verrucosa</ce:italic> (Mill.) H</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Duval. Planta</sb:maintitle></sb:title><sb:volume-nr>65</sb:volume-nr></sb:series><sb:date>1985</sb:date></sb:issue><sb:pages><sb:first-page>1</sb:first-page><sb:last-page>10</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib27"><ce:label>Wasternack et al., 1994</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>C.</ce:given-name><ce:surname>Wasternack</ce:surname></sb:author><sb:author><ce:given-name>R.</ce:given-name><ce:surname>Atzorn</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Blume</ce:surname></sb:author><sb:author><ce:given-name>J.</ce:given-name><ce:surname>Leopold</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Parthier</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Ursolic acid inhibits synthesis of jasmonate-induced proteins in barley leaves</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Phytochemistry</sb:maintitle></sb:title><sb:volume-nr>35</sb:volume-nr></sb:series><sb:date>1994</sb:date></sb:issue><sb:pages><sb:first-page>49</sb:first-page><sb:last-page>54</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib28"><ce:label>Weidhase et al., 1987</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:given-name>P.A.</ce:given-name><ce:surname>Weidhase</ce:surname></sb:author><sb:author><ce:given-name>H.-M.</ce:given-name><ce:surname>Kramell</ce:surname></sb:author><sb:author><ce:given-name>J.</ce:given-name><ce:surname>Lehmann</ce:surname></sb:author><sb:author><ce:given-name>H.W.</ce:given-name><ce:surname>Liebisch</ce:surname></sb:author><sb:author><ce:given-name>W.</ce:given-name><ce:surname>Lerbs</ce:surname></sb:author><sb:author><ce:given-name>B.</ce:given-name><ce:surname>Parthier</ce:surname></sb:author></sb:authors><sb:title><sb:maintitle>Methyljasmonate-induced changes in the polypeptide pattern of senescing barley leaf segments</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Plant Sci.</sb:maintitle></sb:title><sb:volume-nr>51</sb:volume-nr></sb:series><sb:date>1987</sb:date></sb:issue><sb:pages><sb:first-page>171</sb:first-page><sb:last-page>186</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference></ce:bibliography-sec></ce:bibliography></tail></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Alteration of V-type H+-ATPase during methyljasmonate-induced senescence in barley ( Hordeum vulgare L. cv. Salome)</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Alteration of V-type H</title></titleInfo><name type="personal"><namePart type="given">R.</namePart><namePart type="family">Ratajczak</namePart><affiliation>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">I.</namePart><namePart type="family">Feussner</namePart><affiliation>Institut fur Botanik, Technische Universität Darmstadt, Schnittspahnstr. 3-5, D-64287 Darmstadt, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">B.</namePart><namePart type="family">Hause</namePart><affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.</namePart><namePart type="family">Böhm</namePart><affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">B.</namePart><namePart type="family">Parthier</namePart><affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">C.</namePart><namePart type="family">Wasternack</namePart><affiliation>Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany</affiliation><affiliation>Correspondence.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1998</dateIssued><copyrightDate encoding="w3cdtf">1998</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract>In barley leaves, the application of (−)-jasmonic acid or its methyl ester (JAME) induces a senescencelike phenotype. This is accompanied by the synthesis of abundant proteins, so-called jasmonate-induced proteins (JlPs). Here, we show that modifications of vacuolar H+-ATPase (V-ATPase) subunits are jasmo-nate inducible. Using immunofluorescence analysis, we demonstrate that V-ATPase of barley leaves is exclusively located at the tonoplast also upon JAME treatment. Total ATP-hydrolysis activity of microsomal fractions increased by a factor of 10 during 72 h of JAME-treatment, while Bafilomycin Ai-sensitive ATP-hydrolysis activity, which is usually referred to V-ATPase activity, increased by a factor of about 2 in tono-plast-enriched membrane fractions. Moreover, due to JAME treatment there was a pronounced increase in ATP-hydrolysis activity at pH 6.2. This activity was not affected by inhibitors of P-, F-, or V-ATPases. However, biochemical analysis of partially purified V-ATPase suggests, that this activity might be due at least in part to the V-ATPase. JAME-treatment seems to change biochemical properties of the V-ATPase, i.e. a shift of the pH optimum of activity to a more acidic pH and a decrease in Bafilomycin A1 sensitivity. This is accompanied by the appearance of several additional forms of V-ATPase subunits which might represent either different isoforms or post-translationally modified proteins. We suggest that these changes in properties of the V-ATPase, which is involved in house-keeping and stress responses, may be due to JAME-induced senescence to overcome concomitant changes of the vacuolar membrane.</abstract><subject lang="en"><genre>Key words</genre><topic>Altered subunits</topic><topic>biochemical properties</topic><topic>jasmonates</topic><topic>V-ATPase</topic></subject><subject lang="en"><genre>Abbreviations</genre><topic>BSA : Bovine serum albumin</topic><topic>DAPI : 4,6-Diamidino-2-phenylindole</topic><topic>DTT : Dithiothreitol</topic><topic>EDTA : Ethylendiaminetetraacetic acid</topic><topic>FITC : Fluorescein-5-isothiocyanate</topic><topic>HEPES : N-(2-Hydroxyethyl)piperazine-N′-(2-ethanesulfonic acid)</topic><topic>JAME : Jasmonic acid methylester</topic><topic>J1Ps : Jasmonate-induced proteins</topic><topic>MES : 2-(N-Morpholino)ethanesulfonic acid</topic><topic>PBS : Phosphate buffered saline</topic><topic>PEG : polyethylene glycol</topic><topic>SDS-PAGE : Sodium dodecyl sulphate-polyacrylamide gel electrophoresis</topic><topic>Tris : Tris(hydroxymethyl)aminomethane</topic><topic>V-ATPase : Vacuolar-type H+-ATPase</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Plant Physiology</title></titleInfo><titleInfo type="abbreviated"><title>JPLPH</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">1998</dateIssued></originInfo><identifier type="ISSN">0176-1617</identifier><identifier type="PII">S0176-1617(98)X8122-8</identifier><part><date>1998</date><detail type="volume"><number>152</number><caption>vol.</caption></detail><detail type="issue"><number>2–3</number><caption>no.</caption></detail><extent unit="issue pages"><start>131</start><end>352</end></extent><extent unit="pages"><start>199</start><end>206</end></extent></part></relatedItem><identifier type="istex">AA2F4CB65804434D1086F7A002E03B9C18400E28</identifier><identifier type="DOI">10.1016/S0176-1617(98)80133-8</identifier><identifier type="PII">S0176-1617(98)80133-8</identifier><identifier type="ArticleID">80133</identifier><accessCondition type="use and reproduction" contentType="copyright">©1998 Gustav Fischer Verlag, Jena</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Gustav Fischer Verlag, Jena, ©1998</recordOrigin></recordInfo></mods></metadata><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/AA2F4CB65804434D1086F7A002E03B9C18400E28/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">PLANT SCIENCES</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Bois/explor/OrangerV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000749 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 000749 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Bois
|area= OrangerV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:AA2F4CB65804434D1086F7A002E03B9C18400E28
|texte= Alteration of V-type H+-ATPase during methyljasmonate-induced senescence in barley ( Hordeum vulgare L. cv. Salome)
}}
| This area was generated with Dilib version V0.6.25. |  |