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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The Arabidopsis F-Box Protein SLEEPY1 Targets Gibberellin Signaling Repressors for Gibberellin-Induced Degradation<xref ref-type="fn" rid="fn2">W⃞</xref></title><author><name sortKey="Dill, Alyssa" sort="Dill, Alyssa" uniqKey="Dill A" first="Alyssa" last="Dill">Alyssa Dill</name><affiliation><nlm:aff id="aff1">Department of Biology, Duke University, Durham, North Carolina 27708-1000</nlm:aff></affiliation></author><author><name sortKey="Thomas, Stephen G" sort="Thomas, Stephen G" uniqKey="Thomas S" first="Stephen G." last="Thomas">Stephen G. Thomas</name><affiliation><nlm:aff id="aff1">Department of Biology, Duke University, Durham, North Carolina 27708-1000</nlm:aff></affiliation></author><author><name sortKey="Hu, Jianhong" sort="Hu, Jianhong" uniqKey="Hu J" first="Jianhong" last="Hu">Jianhong Hu</name><affiliation><nlm:aff id="aff1">Department of Biology, Duke University, Durham, North Carolina 27708-1000</nlm:aff></affiliation></author><author><name sortKey="Steber, Camille M" sort="Steber, Camille M" uniqKey="Steber C" first="Camille M." last="Steber">Camille M. Steber</name><affiliation><nlm:aff id="aff2">U.S. Department of Agriculture Agricultural Research Service, Washington State University, Pullman, Washington 99164-6420</nlm:aff></affiliation></author><author><name sortKey="Sun, Tai Ping" sort="Sun, Tai Ping" uniqKey="Sun T" first="Tai-Ping" last="Sun">Tai-Ping Sun</name><affiliation><nlm:aff id="aff1">Department of Biology, Duke University, Durham, North Carolina 27708-1000</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">15155881</idno><idno type="pmc">490034</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC490034</idno><idno type="RBID">PMC:490034</idno><idno type="doi">10.1105/tpc.020958</idno><date when="2004">2004</date><idno type="wicri:Area/Pmc/Corpus">000784</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The Arabidopsis F-Box Protein SLEEPY1 Targets Gibberellin Signaling Repressors for Gibberellin-Induced Degradation<xref ref-type="fn" rid="fn2">W⃞</xref></title><author><name sortKey="Dill, Alyssa" sort="Dill, Alyssa" uniqKey="Dill A" first="Alyssa" last="Dill">Alyssa Dill</name><affiliation><nlm:aff id="aff1">Department of Biology, Duke University, Durham, North Carolina 27708-1000</nlm:aff></affiliation></author><author><name sortKey="Thomas, Stephen G" sort="Thomas, Stephen G" uniqKey="Thomas S" first="Stephen G." last="Thomas">Stephen G. Thomas</name><affiliation><nlm:aff id="aff1">Department of Biology, Duke University, Durham, North Carolina 27708-1000</nlm:aff></affiliation></author><author><name sortKey="Hu, Jianhong" sort="Hu, Jianhong" uniqKey="Hu J" first="Jianhong" last="Hu">Jianhong Hu</name><affiliation><nlm:aff id="aff1">Department of Biology, Duke University, Durham, North Carolina 27708-1000</nlm:aff></affiliation></author><author><name sortKey="Steber, Camille M" sort="Steber, Camille M" uniqKey="Steber C" first="Camille M." last="Steber">Camille M. Steber</name><affiliation><nlm:aff id="aff2">U.S. Department of Agriculture Agricultural Research Service, Washington State University, Pullman, Washington 99164-6420</nlm:aff></affiliation></author><author><name sortKey="Sun, Tai Ping" sort="Sun, Tai Ping" uniqKey="Sun T" first="Tai-Ping" last="Sun">Tai-Ping Sun</name><affiliation><nlm:aff id="aff1">Department of Biology, Duke University, Durham, North Carolina 27708-1000</nlm:aff></affiliation></author></analytic><series><title level="j">The Plant Cell</title><idno type="ISSN">1040-4651</idno><idno type="eISSN">1532-298X</idno><imprint><date when="2004">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The nuclear DELLA proteins are highly conserved repressors of hormone gibberellin (GA) signaling in plants. In <italic>Arabidopsis thaliana</italic>, GA derepresses its signaling pathway by inducing proteolysis of the DELLA protein REPRESSOR OF <italic>ga1-3</italic> (RGA). <italic>SLEEPY1</italic> (<italic>SLY1</italic>) encodes an F-box–containing protein, and the loss-of-function <italic>sly1</italic> mutant has a GA-insensitive dwarf phenotype and accumulates a high level of RGA. These findings suggested that SLY1 recruits RGA to the SCF<sup>SLY1</sup> E3 ligase complex for ubiquitination and subsequent degradation by the 26S proteasome. In this report, we provide new insight into the molecular mechanism of how SLY1 interacts with the DELLA proteins for controlling GA response. By yeast two-hybrid and in vitro pull-down assays, we demonstrated that SLY1 interacts directly with RGA and GA INSENSITIVE (GAI, a closely related DELLA protein) via their C-terminal GRAS domain. The <italic>rga</italic> and <italic>gai</italic> null mutations additively suppressed the recessive <italic>sly1</italic> mutant phenotype, further supporting the model that SCF<sup>SLY1</sup> targets both RGA and GAI for degradation. The N-terminal DELLA domain of RGA previously was shown to be essential for GA-induced degradation. However, we found that this DELLA domain is not required for protein–protein interaction with SLY1 in yeast (<italic>Saccharomyces cerevisiae</italic>), suggesting that its role is in a GA-triggered conformational change of the DELLA proteins. We also identified a novel gain-of-function <italic>sly1-d</italic> mutation that increased GA signaling by reducing the levels of the DELLA protein in plants. This effect of <italic>sly1-d</italic> appears to be caused by an enhanced interaction between sly1-d and the DELLA proteins.</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 Cell</journal-id><journal-id journal-id-type="publisher-id">plantcell</journal-id><journal-title>The Plant Cell</journal-title><issn pub-type="ppub">1040-4651</issn><issn pub-type="epub">1532-298X</issn><publisher><publisher-name>American Society of Plant Biologists</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">15155881</article-id><article-id pub-id-type="pmc">490034</article-id><article-id pub-id-type="publisher-id">020958</article-id><article-id pub-id-type="doi">10.1105/tpc.020958</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Articles</subject></subj-group></article-categories><title-group><article-title>The Arabidopsis F-Box Protein SLEEPY1 Targets Gibberellin Signaling Repressors for Gibberellin-Induced Degradation<xref ref-type="fn" rid="fn2">W⃞</xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Dill</surname><given-names>Alyssa</given-names></name><xref ref-type="aff" rid="aff1">a</xref><xref ref-type="fn" rid="fn1">1</xref></contrib><contrib contrib-type="author"><name><surname>Thomas</surname><given-names>Stephen G.</given-names></name><xref ref-type="aff" rid="aff1">a</xref><xref ref-type="fn" rid="fn1">1</xref></contrib><contrib contrib-type="author"><name><surname>Hu</surname><given-names>Jianhong</given-names></name><xref ref-type="aff" rid="aff1">a</xref></contrib><contrib contrib-type="author"><name><surname>Steber</surname><given-names>Camille M.</given-names></name><xref ref-type="aff" rid="aff2">b</xref></contrib><contrib contrib-type="author"><name><surname>Sun</surname><given-names>Tai-ping</given-names></name><xref ref-type="aff" rid="aff1">a</xref><xref ref-type="corresp" rid="cor1">2</xref></contrib></contrib-group><aff id="aff1"><label>a</label>Department of Biology, Duke University, Durham, North Carolina 27708-1000</aff><aff id="aff2"><label>b</label>U.S. Department of Agriculture Agricultural Research Service, Washington State University, Pullman, Washington 99164-6420</aff><author-notes><fn id="fn1"><label>1</label><p>These authors contributed equally to this work.</p></fn><fn id="cor1"><label>2</label><p>To whom correspondence should be addressed. E-mail <email>tps@duke.edu</email>; fax 919-613-8177.</p></fn></author-notes><pub-date pub-type="ppub"><month>6</month><year>2004</year></pub-date><volume>16</volume><issue>6</issue><fpage>1392</fpage><lpage>1405</lpage><history><date date-type="received"><day>13</day><month>1</month><year>2004</year></date><date date-type="accepted"><day>8</day><month>3</month><year>2004</year></date></history><copyright-statement>Copyright © 2004, American Society of Plant Biologists</copyright-statement><copyright-year>2004</copyright-year><abstract><p>The nuclear DELLA proteins are highly conserved repressors of hormone gibberellin (GA) signaling in plants. In <italic>Arabidopsis thaliana</italic>, GA derepresses its signaling pathway by inducing proteolysis of the DELLA protein REPRESSOR OF <italic>ga1-3</italic> (RGA). <italic>SLEEPY1</italic> (<italic>SLY1</italic>) encodes an F-box–containing protein, and the loss-of-function <italic>sly1</italic> mutant has a GA-insensitive dwarf phenotype and accumulates a high level of RGA. These findings suggested that SLY1 recruits RGA to the SCF<sup>SLY1</sup> E3 ligase complex for ubiquitination and subsequent degradation by the 26S proteasome. In this report, we provide new insight into the molecular mechanism of how SLY1 interacts with the DELLA proteins for controlling GA response. By yeast two-hybrid and in vitro pull-down assays, we demonstrated that SLY1 interacts directly with RGA and GA INSENSITIVE (GAI, a closely related DELLA protein) via their C-terminal GRAS domain. The <italic>rga</italic> and <italic>gai</italic> null mutations additively suppressed the recessive <italic>sly1</italic> mutant phenotype, further supporting the model that SCF<sup>SLY1</sup> targets both RGA and GAI for degradation. The N-terminal DELLA domain of RGA previously was shown to be essential for GA-induced degradation. However, we found that this DELLA domain is not required for protein–protein interaction with SLY1 in yeast (<italic>Saccharomyces cerevisiae</italic>), suggesting that its role is in a GA-triggered conformational change of the DELLA proteins. We also identified a novel gain-of-function <italic>sly1-d</italic> mutation that increased GA signaling by reducing the levels of the DELLA protein in plants. This effect of <italic>sly1-d</italic> appears to be caused by an enhanced interaction between sly1-d and the DELLA proteins.</p></abstract></article-meta><notes><fn-group><fn id="fn2"><label>W⃞</label><p>Online version contains Web-only data.</p></fn><fn><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="www.plantcell.org">www.plantcell.org</ext-link>) is: Tai-ping Sun (<email>tps@duke.edu</email>).</p><p>Article, publication date, and citation information can be found at <ext-link ext-link-type="uri" xlink:href="www.plantcell.org/cgi/doi/10.1105/tpc.020958">www.plantcell.org/cgi/doi/10.1105/tpc.020958</ext-link>.</p></fn></fn-group></notes></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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