Membrane Topology of the MotA Protein of Escherichia coil
Identifieur interne : 004108 ( Istex/Corpus ); précédent : 004107; suivant : 004109Membrane Topology of the MotA Protein of Escherichia coil
Auteurs : Jiadong Zhou ; Robert T. Fazzio ; David F. BlairSource :
- Journal of Molecular Biology [ 0022-2836 ] ; 1995.
English descriptors
- KwdEn :
- Teeft :
- Agellar motor, Amino, Berg, Blair, Blair berg, Coli, Coli figure, Cytoplasmic, Electrophoresed, Encodes mota, Escherichia, Escherichia coli, Hydrophobic segments, Intact spheroplasts, Large cytoplasmic domain, Main features, Membrane, Mota, Mota protein, Mota topology, Mota variants, Mutant, Mutation, Natl acad, Other positions, Periplasm, Periplasmic, Periplasmic segment, Periplasmic segments, Periplasmic side, Plasmid, Protease, Reaction rate, Room temperature, Short segments, Spheroplast, Spheroplasts, Topology, Uorescein.
Abstract
Abstract: The MotA protein ofEscherichia coliis a component of the flagella that functions together with the MotB protein in transmembrane proton conduction. It is an integral membrane protein, with four hydrophobic segments that might traverse the membrane and two short segments that are predicted to be in the periplasm. In a previous study of the accessibility of MotA to various proteases, evidence for periplasmic segments was not obtained, probably because they are small. Here, we report site-directed sulfhydryl labeling experiments which show that two segments of MotA are exposed on the periplasmic side of the membrane, while the rest of the protein is in the cytoplasm. These experiments establish that the main features of the suggested model for MotA topology are correct, furnishing a basis for more detailed structure-function studies of the MotA/MotB proton channel.
Url:
DOI: 10.1006/jmbi.1995.0431
Links to Exploration step
ISTEX:F93C96C718DBE95EFFB40501F6A19680562B91A9Le document en format XML
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Blair</name><affiliation><mods:affiliation>Department of Biology, University of Utah, Salt Lake City, UT 84112, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="ISSN">0022-2836</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995">1995</date><biblScope unit="volume">251</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="237">237</biblScope><biblScope unit="page" to="242">242</biblScope></imprint><idno type="ISSN">0022-2836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-2836</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ion channels</term><term>membrane proteins</term><term>topology</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Agellar motor</term><term>Amino</term><term>Berg</term><term>Blair</term><term>Blair berg</term><term>Coli</term><term>Coli figure</term><term>Cytoplasmic</term><term>Electrophoresed</term><term>Encodes mota</term><term>Escherichia</term><term>Escherichia coli</term><term>Hydrophobic segments</term><term>Intact spheroplasts</term><term>Large cytoplasmic domain</term><term>Main features</term><term>Membrane</term><term>Mota</term><term>Mota protein</term><term>Mota topology</term><term>Mota variants</term><term>Mutant</term><term>Mutation</term><term>Natl acad</term><term>Other positions</term><term>Periplasm</term><term>Periplasmic</term><term>Periplasmic segment</term><term>Periplasmic segments</term><term>Periplasmic side</term><term>Plasmid</term><term>Protease</term><term>Reaction rate</term><term>Room temperature</term><term>Short segments</term><term>Spheroplast</term><term>Spheroplasts</term><term>Topology</term><term>Uorescein</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The MotA protein ofEscherichia coliis a component of the flagella that functions together with the MotB protein in transmembrane proton conduction. It is an integral membrane protein, with four hydrophobic segments that might traverse the membrane and two short segments that are predicted to be in the periplasm. In a previous study of the accessibility of MotA to various proteases, evidence for periplasmic segments was not obtained, probably because they are small. Here, we report site-directed sulfhydryl labeling experiments which show that two segments of MotA are exposed on the periplasmic side of the membrane, while the rest of the protein is in the cytoplasm. 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Fazzio</name><affiliations><json:string>Department of Biology, University of Utah, Salt Lake City, UT 84112, USA</json:string></affiliations></json:item><json:item><name>David F. Blair</name><affiliations><json:string>Department of Biology, University of Utah, Salt Lake City, UT 84112, USA</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>ion channels</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>membrane proteins</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>topology</value></json:item></subject><arkIstex>ark:/67375/6H6-9B35WX58-P</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The MotA protein ofEscherichia coliis a component of the flagella that functions together with the MotB protein in transmembrane proton conduction. 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These experiments establish that the main features of the suggested model for MotA topology are correct, furnishing a basis for more detailed structure-function studies of the MotA/MotB proton channel.</abstract><qualityIndicators><score>7.572</score><pdfWordCount>3952</pdfWordCount><pdfCharCount>23983</pdfCharCount><pdfVersion>1.1</pdfVersion><pdfPageCount>6</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>false</refBibsNative><abstractWordCount>135</abstractWordCount><abstractCharCount>884</abstractCharCount><keywordCount>3</keywordCount></qualityIndicators><title>Membrane Topology of the MotA Protein of Escherichia coil</title><pmid><json:string>7643400</json:string></pmid><pii><json:string>S0022-2836(85)70431-7</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Journal of Molecular Biology</title><language><json:string>unknown</json:string></language><publicationDate>1995</publicationDate><issn><json:string>0022-2836</json:string></issn><pii><json:string>S0022-2836(00)X0416-0</json:string></pii><volume>251</volume><issue>2</issue><pages><first>237</first><last>242</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1995</json:string></date><geogName></geogName><orgName><json:string>National Cancer Institute</json:string><json:string>California Institute of Technology</json:string><json:string>Department of Biology</json:string><json:string>Amersham</json:string><json:string>University of Utah</json:string><json:string>National Institute of General Medical Sciences</json:string><json:string>Yale University</json:string><json:string>Hughes Undergraduate Research Program</json:string></orgName><orgName_funder><json:string>Hughes Undergraduate Research Program</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>David Goldenberg</json:string><json:string>Eckstein</json:string><json:string>Jiadong Zhou</json:string><json:string>H. 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(1984)</json:string><json:string>Hucho et al., 1994</json:string><json:string>Schuster & Khan, 1994</json:string><json:string>reviewed by Macnab, 1992</json:string><json:string>Taylor et al., 1985</json:string><json:string>Doering, 1992</json:string><json:string>Mirel et al., 1992</json:string><json:string>Studier & Moffatt, 1986</json:string><json:string>Hueck et al., 1993</json:string><json:string>Larsen et al., 1974</json:string><json:string>Wilson & Macnab, 1988</json:string><json:string>Falke et al. (1988)</json:string><json:string>Hirota & Imae, 1983</json:string><json:string>Dean et al., 1984</json:string><json:string>Sambrook et al. (1989)</json:string><json:string>Chun, 1988</json:string><json:string>Smyth et al., 1964</json:string><json:string>fluorescein 5-maleimide; Hoagland, 1994</json:string><json:string>Blair, 1995</json:string><json:string>Blair & Berg, 1991</json:string><json:string>Sharp et al., 1995</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-9B35WX58-P</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Biology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string><json:string>4 - biochimie analytique, structurale et metabolique</json:string></inist></categories><publicationDate>1995</publicationDate><copyrightDate>1995</copyrightDate><doi><json:string>10.1006/jmbi.1995.0431</json:string></doi><id>F93C96C718DBE95EFFB40501F6A19680562B91A9</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-9B35WX58-P/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-9B35WX58-P/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-9B35WX58-P/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Membrane Topology of the MotA Protein of Escherichia coil</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>©1995 Academic Press</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</p></availability><date>1995</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Membrane Topology of the MotA Protein of Escherichia coil</title><author xml:id="author-0000"><persName><forename type="first">Jiadong</forename><surname>Zhou</surname></persName><affiliation>Department of Biology, University of Utah, Salt Lake City, UT 84112, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Robert T.</forename><surname>Fazzio</surname></persName><affiliation>Department of Biology, University of Utah, Salt Lake City, UT 84112, USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">David F.</forename><surname>Blair</surname></persName><note type="correspondence"><p>Corresponding author</p></note><affiliation>Department of Biology, University of Utah, Salt Lake City, UT 84112, USA</affiliation></author><idno type="istex">F93C96C718DBE95EFFB40501F6A19680562B91A9</idno><idno type="ark">ark:/67375/6H6-9B35WX58-P</idno><idno type="DOI">10.1006/jmbi.1995.0431</idno><idno type="PII">S0022-2836(85)70431-7</idno></analytic><monogr><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="pISSN">0022-2836</idno><idno type="PII">S0022-2836(00)X0416-0</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995"></date><biblScope unit="volume">251</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="237">237</biblScope><biblScope unit="page" to="242">242</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1995</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The MotA protein ofEscherichia coliis a component of the flagella that functions together with the MotB protein in transmembrane proton conduction. It is an integral membrane protein, with four hydrophobic segments that might traverse the membrane and two short segments that are predicted to be in the periplasm. In a previous study of the accessibility of MotA to various proteases, evidence for periplasmic segments was not obtained, probably because they are small. Here, we report site-directed sulfhydryl labeling experiments which show that two segments of MotA are exposed on the periplasmic side of the membrane, while the rest of the protein is in the cytoplasm. These experiments establish that the main features of the suggested model for MotA topology are correct, furnishing a basis for more detailed structure-function studies of the MotA/MotB proton channel.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>ion channels</term></item><item><term>membrane proteins</term></item><item><term>topology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1995">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-9B35WX58-P/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier converted-article found"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>YJMBI</jid><aid>70431</aid><ce:pii>S0022-2836(85)70431-7</ce:pii><ce:doi>10.1006/jmbi.1995.0431</ce:doi><ce:copyright type="full-transfer" year="1995">Academic Press</ce:copyright></item-info><head><ce:title>Membrane Topology of the MotA Protein of<ce:italic>Escherichia coil</ce:italic></ce:title><ce:author-group><ce:author><ce:given-name>Jiadong</ce:given-name><ce:surname>Zhou</ce:surname><ce:cross-ref refid="A1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Robert T.</ce:given-name><ce:surname>Fazzio</ce:surname><ce:cross-ref refid="A1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>David F.</ce:given-name><ce:surname>Blair</ce:surname><ce:cross-ref refid="A1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>*</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="A1"><ce:label>a</ce:label><ce:textfn>Department of Biology, University of Utah, Salt Lake City, UT 84112, USA</ce:textfn></ce:affiliation><ce:footnote id="FN1"><ce:label>f1</ce:label><ce:note-para>Corresponding author</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="29" month="12" year="1995"></ce:date-received><ce:date-accepted day="22" month="5" year="1995"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The MotA protein of<ce:italic>Escherichia coli</ce:italic>is a component of the flagella that functions together with the MotB protein in transmembrane proton conduction. It is an integral membrane protein, with four hydrophobic segments that might traverse the membrane and two short segments that are predicted to be in the periplasm. In a previous study of the accessibility of MotA to various proteases, evidence for periplasmic segments was not obtained, probably because they are small. Here, we report site-directed sulfhydryl labeling experiments which show that two segments of MotA are exposed on the periplasmic side of the membrane, while the rest of the protein is in the cytoplasm. These experiments establish that the main features of the suggested model for MotA topology are correct, furnishing a basis for more detailed structure-function studies of the MotA/MotB proton channel.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>ion channels</ce:text></ce:keyword><ce:keyword><ce:text>membrane proteins</ce:text></ce:keyword><ce:keyword><ce:text>topology</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Membrane Topology of the MotA Protein of Escherichia coil</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Membrane Topology of the MotA Protein of</title></titleInfo><name type="personal"><namePart type="given">Jiadong</namePart><namePart type="family">Zhou</namePart><affiliation>Department of Biology, University of Utah, Salt Lake City, UT 84112, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Robert T.</namePart><namePart type="family">Fazzio</namePart><affiliation>Department of Biology, University of Utah, Salt Lake City, UT 84112, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David F.</namePart><namePart type="family">Blair</namePart><affiliation>Department of Biology, University of Utah, Salt Lake City, UT 84112, USA</affiliation><description>Corresponding author</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1995</dateIssued><copyrightDate encoding="w3cdtf">1995</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The MotA protein ofEscherichia coliis a component of the flagella that functions together with the MotB protein in transmembrane proton conduction. It is an integral membrane protein, with four hydrophobic segments that might traverse the membrane and two short segments that are predicted to be in the periplasm. In a previous study of the accessibility of MotA to various proteases, evidence for periplasmic segments was not obtained, probably because they are small. Here, we report site-directed sulfhydryl labeling experiments which show that two segments of MotA are exposed on the periplasmic side of the membrane, while the rest of the protein is in the cytoplasm. These experiments establish that the main features of the suggested model for MotA topology are correct, furnishing a basis for more detailed structure-function studies of the MotA/MotB proton channel.</abstract><subject lang="en"><genre>Keywords</genre><topic>ion channels</topic><topic>membrane proteins</topic><topic>topology</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Molecular Biology</title></titleInfo><titleInfo type="abbreviated"><title>YJMBI</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1995</dateIssued></originInfo><identifier type="ISSN">0022-2836</identifier><identifier type="PII">S0022-2836(00)X0416-0</identifier><part><date>1995</date><detail type="volume"><number>251</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>191</start><end>326</end></extent><extent unit="pages"><start>237</start><end>242</end></extent></part></relatedItem><identifier type="istex">F93C96C718DBE95EFFB40501F6A19680562B91A9</identifier><identifier type="ark">ark:/67375/6H6-9B35WX58-P</identifier><identifier type="DOI">10.1006/jmbi.1995.0431</identifier><identifier type="PII">S0022-2836(85)70431-7</identifier><accessCondition type="use and reproduction" contentType="copyright">©1995 Academic Press</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource><recordOrigin>Academic Press, ©1995</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-9B35WX58-P/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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