β-Amylase1 and β-Amylase3 Are Plastidic Starch Hydrolases in Arabidopsis That Seem to Be Adapted for Different Thermal, pH, and Stress Conditions1[W][OPEN]
Identifieur interne : 000D20 ( Pmc/Corpus ); précédent : 000D19; suivant : 000D21β-Amylase1 and β-Amylase3 Are Plastidic Starch Hydrolases in Arabidopsis That Seem to Be Adapted for Different Thermal, pH, and Stress Conditions1[W][OPEN]
Auteurs : Jonathan D. Monroe ; Amanda R. Storm ; Elizabeth M. Badley ; Michael D. Lehman ; Samantha M. Platt ; Lauren K. Saunders ; Jonathan M. Schmitz ; Catherine E. TorresSource :
- Plant Physiology [ 0032-0889 ] ; 2014.
Abstract
Url:
DOI: 10.1104/pp.114.246421
PubMed: 25293962
PubMed Central: 4256876
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PMC:4256876Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en"><italic>β</italic>-Amylase1 and <italic>β</italic>-Amylase3 Are Plastidic Starch Hydrolases in Arabidopsis That Seem to Be Adapted for Different Thermal, pH, and Stress Conditions<xref ref-type="fn" rid="fn1"><sup>1</sup></xref><xref ref-type="fn" rid="fn2"><sup>[W]</sup></xref><xref ref-type="fn" rid="fn3"><sup>[OPEN]</sup></xref></title><author><name sortKey="Monroe, Jonathan D" sort="Monroe, Jonathan D" uniqKey="Monroe J" first="Jonathan D." last="Monroe">Jonathan D. Monroe</name></author><author><name sortKey="Storm, Amanda R" sort="Storm, Amanda R" uniqKey="Storm A" first="Amanda R." last="Storm">Amanda R. Storm</name></author><author><name sortKey="Badley, Elizabeth M" sort="Badley, Elizabeth M" uniqKey="Badley E" first="Elizabeth M." last="Badley">Elizabeth M. Badley</name></author><author><name sortKey="Lehman, Michael D" sort="Lehman, Michael D" uniqKey="Lehman M" first="Michael D." last="Lehman">Michael D. Lehman</name></author><author><name sortKey="Platt, Samantha M" sort="Platt, Samantha M" uniqKey="Platt S" first="Samantha M." last="Platt">Samantha M. Platt</name></author><author><name sortKey="Saunders, Lauren K" sort="Saunders, Lauren K" uniqKey="Saunders L" first="Lauren K." last="Saunders">Lauren K. Saunders</name></author><author><name sortKey="Schmitz, Jonathan M" sort="Schmitz, Jonathan M" uniqKey="Schmitz J" first="Jonathan M." last="Schmitz">Jonathan M. Schmitz</name></author><author><name sortKey="Torres, Catherine E" sort="Torres, Catherine E" uniqKey="Torres C" first="Catherine E." last="Torres">Catherine E. Torres</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25293962</idno><idno type="pmc">4256876</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4256876</idno><idno type="RBID">PMC:4256876</idno><idno type="doi">10.1104/pp.114.246421</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000D20</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main"><italic>β</italic>-Amylase1 and <italic>β</italic>-Amylase3 Are Plastidic Starch Hydrolases in Arabidopsis That Seem to Be Adapted for Different Thermal, pH, and Stress Conditions<xref ref-type="fn" rid="fn1"><sup>1</sup></xref><xref ref-type="fn" rid="fn2"><sup>[W]</sup></xref><xref ref-type="fn" rid="fn3"><sup>[OPEN]</sup></xref></title><author><name sortKey="Monroe, Jonathan D" sort="Monroe, Jonathan D" uniqKey="Monroe J" first="Jonathan D." last="Monroe">Jonathan D. Monroe</name></author><author><name sortKey="Storm, Amanda R" sort="Storm, Amanda R" uniqKey="Storm A" first="Amanda R." last="Storm">Amanda R. Storm</name></author><author><name sortKey="Badley, Elizabeth M" sort="Badley, Elizabeth M" uniqKey="Badley E" first="Elizabeth M." last="Badley">Elizabeth M. Badley</name></author><author><name sortKey="Lehman, Michael D" sort="Lehman, Michael D" uniqKey="Lehman M" first="Michael D." last="Lehman">Michael D. Lehman</name></author><author><name sortKey="Platt, Samantha M" sort="Platt, Samantha M" uniqKey="Platt S" first="Samantha M." last="Platt">Samantha M. Platt</name></author><author><name sortKey="Saunders, Lauren K" sort="Saunders, Lauren K" uniqKey="Saunders L" first="Lauren K." last="Saunders">Lauren K. Saunders</name></author><author><name sortKey="Schmitz, Jonathan M" sort="Schmitz, Jonathan M" uniqKey="Schmitz J" first="Jonathan M." last="Schmitz">Jonathan M. Schmitz</name></author><author><name sortKey="Torres, Catherine E" sort="Torres, Catherine E" uniqKey="Torres C" first="Catherine E." last="Torres">Catherine E. Torres</name></author></analytic><series><title level="j">Plant Physiology</title><idno type="ISSN">0032-0889</idno><idno type="eISSN">1532-2548</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><italic>A β-amylase that works during the day and under osmotic stress is more active at high pH and more thermostable than a mesophyll cell β-amylase that works at night and under cold stress</italic>.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Plant Physiol</journal-id><journal-id journal-id-type="iso-abbrev">Plant Physiol</journal-id><journal-id journal-id-type="hwp">plantphysiol</journal-id><journal-id journal-id-type="publisher-id">aspb</journal-id><journal-title-group><journal-title>Plant Physiology</journal-title></journal-title-group><issn pub-type="ppub">0032-0889</issn><issn pub-type="epub">1532-2548</issn><publisher><publisher-name>American Society of Plant Biologists</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25293962</article-id><article-id pub-id-type="pmc">4256876</article-id><article-id pub-id-type="publisher-id">246421</article-id><article-id pub-id-type="doi">10.1104/pp.114.246421</article-id><article-categories><subj-group subj-group-type="heading"><subject>Articles</subject><subj-group subj-group-type="heading"><subject>Biochemistry and Metabolism</subject></subj-group></subj-group></article-categories><title-group><article-title><italic>β</italic>-Amylase1 and <italic>β</italic>-Amylase3 Are Plastidic Starch Hydrolases in Arabidopsis That Seem to Be Adapted for Different Thermal, pH, and Stress Conditions<xref ref-type="fn" rid="fn1"><sup>1</sup></xref><xref ref-type="fn" rid="fn2"><sup>[W]</sup></xref><xref ref-type="fn" rid="fn3"><sup>[OPEN]</sup></xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Monroe</surname><given-names>Jonathan D.</given-names></name><xref ref-type="corresp" rid="cor1">*</xref></contrib><contrib contrib-type="author"><name><surname>Storm</surname><given-names>Amanda R.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Badley</surname><given-names>Elizabeth M.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Lehman</surname><given-names>Michael D.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Platt</surname><given-names>Samantha M.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Saunders</surname><given-names>Lauren K.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Schmitz</surname><given-names>Jonathan M.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Torres</surname><given-names>Catherine E.</given-names></name></contrib><aff id="aff1">Department of Biology, James Madison University, Harrisonburg, Virginia 22807</aff></contrib-group><author-notes><fn><p><ext-link ext-link-type="uri" xlink:href="http://www.plantphysiol.org/cgi/doi/10.1104/pp.114.246421">www.plantphysiol.org/cgi/doi/10.1104/pp.114.246421</ext-link></p></fn><corresp id="cor1"><label>*</label>Address correspondence to <email>monroejd@jmu.edu</email>.</corresp><fn id="afn1"><p>The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (<ext-link ext-link-type="uri" xlink:href="http://www.plantphysiol.org">www.plantphysiol.org</ext-link>) is: Jonathan D. Monroe (<email>monroejd@jmu.edu</email>).</p></fn></author-notes><pmc-comment>Fake ppub date generated by PMC from publisher pub-date/@pub-type='epub-ppub' </pmc-comment>
<pub-date pub-type="ppub"><month>12</month><year>2014</year></pub-date><pub-date pub-type="epub"><day>07</day><month>10</month><year>2014</year></pub-date><pub-date pub-type="pmc-release"><day>07</day><month>10</month><year>2014</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>166</volume><issue>4</issue><fpage>1748</fpage><lpage>1763</lpage><history><date date-type="received"><day>11</day><month>7</month><year>2014</year></date><date date-type="accepted"><day>06</day><month>10</month><year>2014</year></date></history><permissions><copyright-statement>© 2014 American Society of Plant Biologists. All Rights Reserved.</copyright-statement><copyright-year>2014</copyright-year></permissions><self-uri xlink:role="icon" xlink:href="PP_246421_ic1.gif"></self-uri><self-uri content-type="alt-lang-pdf zh" xlink:href="1748.chinese.pdf"></self-uri><abstract abstract-type="precis"><p><italic>A β-amylase that works during the day and under osmotic stress is more active at high pH and more thermostable than a mesophyll cell β-amylase that works at night and under cold stress</italic>.</p></abstract><abstract><p>Starch degradation in chloroplasts requires β-amylase (BAM) activity, which is encoded by a multigene family. Of nine Arabidopsis (<italic>Arabidopsis thaliana</italic>) <italic>BAM</italic> genes, six encode plastidic enzymes, but only four of these are catalytically active. In vegetative plants, BAM1 acts during the day in guard cells, whereas BAM3 is the dominant activity in mesophyll cells at night. Plastidic BAMs have been difficult to assay in leaf extracts, in part because of a cytosolic activity encoded by <italic>BAM5</italic>. We generated a series of double mutants lacking BAM5 and each of the active plastidic enzymes (BAM1, BAM2, BAM3, and BAM6) and found that most of the plastidic activity in 5-week-old plants was encoded by BAM1 and BAM3. Both of these activities were relatively constant during the day and the night. Analysis of leaf extracts from double mutants and purified BAM1 and BAM3 proteins revealed that these proteins have distinct properties. Using soluble starch as the substrate, BAM1 and BAM3 had optimum activity at pH 6.0 to 6.5, but at high pH, BAM1 was more active than BAM3, consistent with its known daytime role in the guard cell stroma. The optimum temperature for BAM1, which is transcriptionally induced by heat stress, was about 10°C higher than that of BAM3, which is transcriptionally induced by cold stress. The amino acid composition of BAM1 and BAM3 orthologs reflected differences that are consistent with known adaptations of proteins from heat- and cold-adapted organisms, suggesting that these day- and night-active enzymes have undergone thermal adaptation.</p></abstract><counts><page-count count="16"></page-count></counts></article-meta><notes><glossary><title>Glossary</title><def-list><def-item><term id="term1">DTT</term><def id="def1"><p>dithiothreitol</p></def></def-item><def-item><term id="term2">PNPG5</term><def id="def2"><p><italic>p</italic>-nitrophenyl maltopentaose</p></def></def-item><def-item><term id="term3">RT</term><def id="def3"><p>reverse transcription</p></def></def-item></def-list></glossary></notes></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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