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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Chlorophyllase Is a Rate-Limiting Enzyme in Chlorophyll Catabolism and Is Posttranslationally Regulated</title><author><name sortKey="Harpaz Saad, Smadar" sort="Harpaz Saad, Smadar" uniqKey="Harpaz Saad S" first="Smadar" last="Harpaz-Saad">Smadar Harpaz-Saad</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">R.H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agriculture, Food, and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel</nlm:aff></affiliation></author><author><name sortKey="Azoulay, Tamar" sort="Azoulay, Tamar" uniqKey="Azoulay T" first="Tamar" last="Azoulay">Tamar Azoulay</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">R.H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agriculture, Food, and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel</nlm:aff></affiliation></author><author><name sortKey="Arazi, Tzahi" sort="Arazi, Tzahi" uniqKey="Arazi T" first="Tzahi" last="Arazi">Tzahi Arazi</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author><author><name sortKey="Ben Yaakov, Eran" sort="Ben Yaakov, Eran" uniqKey="Ben Yaakov E" first="Eran" last="Ben-Yaakov">Eran Ben-Yaakov</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">R.H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agriculture, Food, and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel</nlm:aff></affiliation></author><author><name sortKey="Mett, Anahit" sort="Mett, Anahit" uniqKey="Mett A" first="Anahit" last="Mett">Anahit Mett</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author><author><name sortKey="Shiboleth, Yoel M" sort="Shiboleth, Yoel M" uniqKey="Shiboleth Y" first="Yoel M." last="Shiboleth">Yoel M. Shiboleth</name><affiliation><nlm:aff id="aff3">Institute of Plant Protection, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author><author><name sortKey="Hortensteiner, Stefan" sort="Hortensteiner, Stefan" uniqKey="Hortensteiner S" first="Stefan" last="Hörtensteiner">Stefan Hörtensteiner</name><affiliation><nlm:aff id="aff4">Institute of Plant Sciences, University of Bern, CH-3013 Bern, Switzerland</nlm:aff></affiliation></author><author><name sortKey="Gidoni, David" sort="Gidoni, David" uniqKey="Gidoni D" first="David" last="Gidoni">David Gidoni</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author><author><name sortKey="Gal On, Amit" sort="Gal On, Amit" uniqKey="Gal On A" first="Amit" last="Gal-On">Amit Gal-On</name><affiliation><nlm:aff id="aff3">Institute of Plant Protection, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author><author><name sortKey="Goldschmidt, Eliezer E" sort="Goldschmidt, Eliezer E" uniqKey="Goldschmidt E" first="Eliezer E." last="Goldschmidt">Eliezer E. Goldschmidt</name><affiliation><nlm:aff id="aff2">R.H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agriculture, Food, and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel</nlm:aff></affiliation></author><author><name sortKey="Eyal, Yoram" sort="Eyal, Yoram" uniqKey="Eyal Y" first="Yoram" last="Eyal">Yoram Eyal</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">17369368</idno><idno type="pmc">1867358</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1867358</idno><idno type="RBID">PMC:1867358</idno><idno type="doi">10.1105/tpc.107.050633</idno><date when="2007">2007</date><idno type="wicri:Area/Pmc/Corpus">000796</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Chlorophyllase Is a Rate-Limiting Enzyme in Chlorophyll Catabolism and Is Posttranslationally Regulated</title><author><name sortKey="Harpaz Saad, Smadar" sort="Harpaz Saad, Smadar" uniqKey="Harpaz Saad S" first="Smadar" last="Harpaz-Saad">Smadar Harpaz-Saad</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">R.H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agriculture, Food, and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel</nlm:aff></affiliation></author><author><name sortKey="Azoulay, Tamar" sort="Azoulay, Tamar" uniqKey="Azoulay T" first="Tamar" last="Azoulay">Tamar Azoulay</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">R.H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agriculture, Food, and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel</nlm:aff></affiliation></author><author><name sortKey="Arazi, Tzahi" sort="Arazi, Tzahi" uniqKey="Arazi T" first="Tzahi" last="Arazi">Tzahi Arazi</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author><author><name sortKey="Ben Yaakov, Eran" sort="Ben Yaakov, Eran" uniqKey="Ben Yaakov E" first="Eran" last="Ben-Yaakov">Eran Ben-Yaakov</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">R.H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agriculture, Food, and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel</nlm:aff></affiliation></author><author><name sortKey="Mett, Anahit" sort="Mett, Anahit" uniqKey="Mett A" first="Anahit" last="Mett">Anahit Mett</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author><author><name sortKey="Shiboleth, Yoel M" sort="Shiboleth, Yoel M" uniqKey="Shiboleth Y" first="Yoel M." last="Shiboleth">Yoel M. Shiboleth</name><affiliation><nlm:aff id="aff3">Institute of Plant Protection, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author><author><name sortKey="Hortensteiner, Stefan" sort="Hortensteiner, Stefan" uniqKey="Hortensteiner S" first="Stefan" last="Hörtensteiner">Stefan Hörtensteiner</name><affiliation><nlm:aff id="aff4">Institute of Plant Sciences, University of Bern, CH-3013 Bern, Switzerland</nlm:aff></affiliation></author><author><name sortKey="Gidoni, David" sort="Gidoni, David" uniqKey="Gidoni D" first="David" last="Gidoni">David Gidoni</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author><author><name sortKey="Gal On, Amit" sort="Gal On, Amit" uniqKey="Gal On A" first="Amit" last="Gal-On">Amit Gal-On</name><affiliation><nlm:aff id="aff3">Institute of Plant Protection, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</nlm:aff></affiliation></author><author><name sortKey="Goldschmidt, Eliezer E" sort="Goldschmidt, Eliezer E" uniqKey="Goldschmidt E" first="Eliezer E." last="Goldschmidt">Eliezer E. Goldschmidt</name><affiliation><nlm:aff id="aff2">R.H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agriculture, Food, and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel</nlm:aff></affiliation></author><author><name sortKey="Eyal, Yoram" sort="Eyal, Yoram" uniqKey="Eyal Y" first="Yoram" last="Eyal">Yoram Eyal</name><affiliation><nlm:aff id="aff1">Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</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="2007">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Chlorophyll is a central player in harvesting light energy for photosynthesis, yet the rate-limiting steps of chlorophyll catabolism and the regulation of the catabolic enzymes remain unresolved. To study the role and regulation of chlorophyllase (Chlase), the first enzyme of the chlorophyll catabolic pathway, we expressed precursor and mature versions of citrus (<italic>Citrus sinensis</italic>) Chlase in two heterologous plant systems: (1) squash (<italic>Cucurbita pepo</italic>) plants using a viral vector expression system; and (2) transiently transformed tobacco (<italic>Nicotiana tabacum</italic>) protoplasts. Expression of full-length citrus Chlase resulted in limited chlorophyll breakdown in protoplasts and no visible leaf phenotype in whole plants, whereas expression of a Chlase version lacking the N-terminal 21 amino acids (ChlaseΔN), which corresponds to the mature protein, led to extensive chlorophyll breakdown in both tobacco protoplasts and squash leaves. ChlaseΔN-expressing squash leaves displayed a dramatic chlorotic phenotype in plants grown under low-intensity light, whereas under natural light a lesion-mimic phenotype occurred, which was demonstrated to follow the accumulation of chlorophyllide, a photodynamic chlorophyll breakdown product. Full-length and mature citrus Chlase versions were localized to the chloroplast membrane fraction in expressing tobacco protoplasts, where processing of the N-terminal 21 amino acids appears to occur. Results obtained in both plant systems suggest that Chlase functions as a rate-limiting enzyme in chlorophyll catabolism controlled via posttranslational regulation.</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-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">17369368</article-id><article-id pub-id-type="pmc">1867358</article-id><article-id pub-id-type="publisher-id">050633</article-id><article-id pub-id-type="doi">10.1105/tpc.107.050633</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Articles</subject></subj-group></article-categories><title-group><article-title>Chlorophyllase Is a Rate-Limiting Enzyme in Chlorophyll Catabolism and Is Posttranslationally Regulated</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Harpaz-Saad</surname><given-names>Smadar</given-names></name><xref ref-type="aff" rid="aff1">a</xref><xref ref-type="aff" rid="aff2">b</xref></contrib><contrib contrib-type="author"><name><surname>Azoulay</surname><given-names>Tamar</given-names></name><xref ref-type="aff" rid="aff1">a</xref><xref ref-type="aff" rid="aff2">b</xref></contrib><contrib contrib-type="author"><name><surname>Arazi</surname><given-names>Tzahi</given-names></name><xref ref-type="aff" rid="aff1">a</xref></contrib><contrib contrib-type="author"><name><surname>Ben-Yaakov</surname><given-names>Eran</given-names></name><xref ref-type="aff" rid="aff1">a</xref><xref ref-type="aff" rid="aff2">b</xref></contrib><contrib contrib-type="author"><name><surname>Mett</surname><given-names>Anahit</given-names></name><xref ref-type="aff" rid="aff1">a</xref></contrib><contrib contrib-type="author"><name><surname>Shiboleth</surname><given-names>Yoel M.</given-names></name><xref ref-type="aff" rid="aff3">c</xref></contrib><contrib contrib-type="author"><name><surname>Hörtensteiner</surname><given-names>Stefan</given-names></name><xref ref-type="aff" rid="aff4">d</xref></contrib><contrib contrib-type="author"><name><surname>Gidoni</surname><given-names>David</given-names></name><xref ref-type="aff" rid="aff1">a</xref></contrib><contrib contrib-type="author"><name><surname>Gal-On</surname><given-names>Amit</given-names></name><xref ref-type="aff" rid="aff3">c</xref></contrib><contrib contrib-type="author"><name><surname>Goldschmidt</surname><given-names>Eliezer E.</given-names></name><xref ref-type="aff" rid="aff2">b</xref></contrib><contrib contrib-type="author"><name><surname>Eyal</surname><given-names>Yoram</given-names></name><xref ref-type="aff" rid="aff1">a</xref><xref ref-type="corresp" rid="cor1">1</xref></contrib></contrib-group><aff id="aff1"><label>a</label>Institute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</aff><aff id="aff2"><label>b</label>R.H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agriculture, Food, and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel</aff><aff id="aff3"><label>c</label>Institute of Plant Protection, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel</aff><aff id="aff4"><label>d</label>Institute of Plant Sciences, University of Bern, CH-3013 Bern, Switzerland</aff><author-notes><fn id="cor1"><label>1</label><p>To whom correspondence should be addressed. E-mail <email>eyalab@volcani.agri.gov.il</email>; fax 972-3-9669583.</p></fn></author-notes><pub-date pub-type="ppub"><month>3</month><year>2007</year></pub-date><volume>19</volume><issue>3</issue><fpage>1007</fpage><lpage>1022</lpage><history><date date-type="received"><day>24</day><month>1</month><year>2007</year></date><date date-type="rev-recd"><day>24</day><month>1</month><year>2007</year></date><date date-type="accepted"><day>27</day><month>2</month><year>2007</year></date></history><permissions><copyright-statement>Copyright © 2007, American Society of Plant Biologists</copyright-statement></permissions><abstract><p>Chlorophyll is a central player in harvesting light energy for photosynthesis, yet the rate-limiting steps of chlorophyll catabolism and the regulation of the catabolic enzymes remain unresolved. To study the role and regulation of chlorophyllase (Chlase), the first enzyme of the chlorophyll catabolic pathway, we expressed precursor and mature versions of citrus (<italic>Citrus sinensis</italic>) Chlase in two heterologous plant systems: (1) squash (<italic>Cucurbita pepo</italic>) plants using a viral vector expression system; and (2) transiently transformed tobacco (<italic>Nicotiana tabacum</italic>) protoplasts. Expression of full-length citrus Chlase resulted in limited chlorophyll breakdown in protoplasts and no visible leaf phenotype in whole plants, whereas expression of a Chlase version lacking the N-terminal 21 amino acids (ChlaseΔN), which corresponds to the mature protein, led to extensive chlorophyll breakdown in both tobacco protoplasts and squash leaves. ChlaseΔN-expressing squash leaves displayed a dramatic chlorotic phenotype in plants grown under low-intensity light, whereas under natural light a lesion-mimic phenotype occurred, which was demonstrated to follow the accumulation of chlorophyllide, a photodynamic chlorophyll breakdown product. Full-length and mature citrus Chlase versions were localized to the chloroplast membrane fraction in expressing tobacco protoplasts, where processing of the N-terminal 21 amino acids appears to occur. Results obtained in both plant systems suggest that Chlase functions as a rate-limiting enzyme in chlorophyll catabolism controlled via posttranslational regulation.</p></abstract></article-meta><notes><fn-group><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: Yoram Eyal (<email>eyalab@volcani.agri.gov.il</email>).</p></fn><fn><p><ext-link ext-link-type="uri" xlink:href="www.plantcell.org/cgi/doi/10.1105/tpc.107.050633">www.plantcell.org/cgi/doi/10.1105/tpc.107.050633</ext-link></p></fn></fn-group></notes></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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