Pheophytin Pheophorbide Hydrolase (Pheophytinase) Is Involved in Chlorophyll Breakdown during Leaf Senescence in Arabidopsis[W][OA]
Identifieur interne : 000978 ( Ncbi/Merge ); précédent : 000977; suivant : 000979Pheophytin Pheophorbide Hydrolase (Pheophytinase) Is Involved in Chlorophyll Breakdown during Leaf Senescence in Arabidopsis[W][OA]
Auteurs : Silvia Schelbert [Suisse] ; Sylvain Aubry [Suisse] ; Bo Burla [Suisse, Corée du Sud] ; Birgit Agne [Suisse] ; Felix Kessler [Suisse] ; Karin Krupinska [Allemagne] ; Stefan Hörtensteiner [Suisse]Source :
- The Plant Cell [ 1040-4651 ] ; 2009.
Abstract
During leaf senescence, chlorophyll is removed from thylakoid membranes and converted in a multistep pathway to colorless breakdown products that are stored in vacuoles. Dephytylation, an early step of this pathway, increases water solubility of the breakdown products. It is widely accepted that chlorophyll is converted into pheophorbide via chlorophyllide. However, chlorophyllase, which converts chlorophyll to chlorophyllide, was found not to be essential for dephytylation in
Url:
DOI: 10.1105/tpc.108.064089
PubMed: 19304936
PubMed Central: 2671698
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<xref ref-type="fn" rid="fn2">[W]</xref>
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<series><title level="j">The Plant Cell</title>
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<front><div type="abstract" xml:lang="en"><p>During leaf senescence, chlorophyll is removed from thylakoid membranes and converted in a multistep pathway to colorless breakdown products that are stored in vacuoles. Dephytylation, an early step of this pathway, increases water solubility of the breakdown products. It is widely accepted that chlorophyll is converted into pheophorbide via chlorophyllide. However, chlorophyllase, which converts chlorophyll to chlorophyllide, was found not to be essential for dephytylation in <italic>Arabidopsis thaliana</italic>
. Here, we identify pheophytinase (PPH), a chloroplast-located and senescence-induced hydrolase widely distributed in algae and land plants. In vitro, <italic>Arabidopsis</italic>
PPH specifically dephytylates the Mg-free chlorophyll pigment, pheophytin (phein), yielding pheophorbide. An <italic>Arabidopsis</italic>
mutant deficient in PPH (<italic>pph-1</italic>
) is unable to degrade chlorophyll during senescence and therefore exhibits a stay-green phenotype. Furthermore, <italic>pph-1</italic>
accumulates phein during senescence. Therefore, PPH is an important component of the chlorophyll breakdown machinery of senescent leaves, and we propose that the sequence of early chlorophyll catabolic reactions be revised. Removal of Mg most likely precedes dephytylation, resulting in the following order of early breakdown intermediates: chlorophyll → pheophytin → pheophorbide. Chlorophyllide, the last precursor of chlorophyll biosynthesis, is most likely not an intermediate of breakdown. Thus, chlorophyll anabolic and catabolic reactions are metabolically separated.</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>
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<article-categories><subj-group subj-group-type="heading"><subject>Research Articles</subject>
</subj-group>
</article-categories>
<title-group><article-title>Pheophytin Pheophorbide Hydrolase (Pheophytinase) Is Involved in Chlorophyll Breakdown during Leaf Senescence in <italic>Arabidopsis</italic>
<xref ref-type="fn" rid="fn2">[W]</xref>
<xref ref-type="fn" rid="fn3">[OA]</xref>
</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Schelbert</surname>
<given-names>Silvia</given-names>
</name>
<xref ref-type="aff" rid="aff1">a</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Aubry</surname>
<given-names>Sylvain</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>Burla</surname>
<given-names>Bo</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>Agne</surname>
<given-names>Birgit</given-names>
</name>
<xref ref-type="aff" rid="aff3">c</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kessler</surname>
<given-names>Felix</given-names>
</name>
<xref ref-type="aff" rid="aff3">c</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Krupinska</surname>
<given-names>Karin</given-names>
</name>
<xref ref-type="aff" rid="aff4">d</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Hörtensteiner</surname>
<given-names>Stefan</given-names>
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<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>
Institute of Plant Biology, University of Zürich, CH-8008 Zurich, Switzerland</aff>
<aff id="aff2"><label>b</label>
Postech-University of Zürich Global Research Laboratory Pohang, University of Science and Technology, Pohang, 790-784, Korea</aff>
<aff id="aff3"><label>c</label>
Laboratoire de Physiologie Végétale, Institut de Biologie, Université de Neuchâtel, CH-2009 Neuchâtel, Switzerland</aff>
<aff id="aff4"><label>d</label>
Institute of Botany and Central Microscopy, University of Kiel, D-24098 Kiel, Germany</aff>
<author-notes><fn id="fn1"><label>1</label>
<p>Current address: Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge CB2 3EA, UK.</p>
</fn>
<fn id="cor1"><label>2</label>
<p>Address correspondence to <email>shorten@botinst.uzh.ch</email>
.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><month>3</month>
<year>2009</year>
</pub-date>
<volume>21</volume>
<issue>3</issue>
<fpage>767</fpage>
<lpage>785</lpage>
<history><date date-type="received"><day>30</day>
<month>10</month>
<year>2008</year>
</date>
<date date-type="rev-recd"><day>12</day>
<month>2</month>
<year>2009</year>
</date>
<date date-type="accepted"><day>8</day>
<month>3</month>
<year>2009</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2009, American Society of Plant Biologists</copyright-statement>
</permissions>
<abstract><p>During leaf senescence, chlorophyll is removed from thylakoid membranes and converted in a multistep pathway to colorless breakdown products that are stored in vacuoles. Dephytylation, an early step of this pathway, increases water solubility of the breakdown products. It is widely accepted that chlorophyll is converted into pheophorbide via chlorophyllide. However, chlorophyllase, which converts chlorophyll to chlorophyllide, was found not to be essential for dephytylation in <italic>Arabidopsis thaliana</italic>
. Here, we identify pheophytinase (PPH), a chloroplast-located and senescence-induced hydrolase widely distributed in algae and land plants. In vitro, <italic>Arabidopsis</italic>
PPH specifically dephytylates the Mg-free chlorophyll pigment, pheophytin (phein), yielding pheophorbide. An <italic>Arabidopsis</italic>
mutant deficient in PPH (<italic>pph-1</italic>
) is unable to degrade chlorophyll during senescence and therefore exhibits a stay-green phenotype. Furthermore, <italic>pph-1</italic>
accumulates phein during senescence. Therefore, PPH is an important component of the chlorophyll breakdown machinery of senescent leaves, and we propose that the sequence of early chlorophyll catabolic reactions be revised. Removal of Mg most likely precedes dephytylation, resulting in the following order of early breakdown intermediates: chlorophyll → pheophytin → pheophorbide. Chlorophyllide, the last precursor of chlorophyll biosynthesis, is most likely not an intermediate of breakdown. Thus, chlorophyll anabolic and catabolic reactions are metabolically separated.</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: Stefan Hörtensteiner (<email>shorten@botinst.uzh.ch</email>
).</p>
</fn>
<fn id="fn2"><label>[W]</label>
<p>Online version contains Web-only data.</p>
</fn>
<fn id="fn3"><label>[OA]</label>
<p>Open Access articles can be viewed online without a subscription.</p>
</fn>
<fn><p><ext-link ext-link-type="uri" xlink:href="www.plantcell.org/cgi/doi/10.1105/tpc.108.064089">www.plantcell.org/cgi/doi/10.1105/tpc.108.064089</ext-link>
</p>
</fn>
</fn-group>
</notes>
</front>
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