Efficient Operation of NAD(P)H Dehydrogenase Requires Supercomplex Formation with Photosystem I via Minor LHCI in Arabidopsis[W]
Identifieur interne : 000C87 ( Pmc/Curation ); précédent : 000C86; suivant : 000C88Efficient Operation of NAD(P)H Dehydrogenase Requires Supercomplex Formation with Photosystem I via Minor LHCI in Arabidopsis[W]
Auteurs : Lianwei Peng [Japon] ; Yoichiro Fukao [Japon] ; Masayuki Fujiwara [Japon] ; Tsuneaki Takami [Japon] ; Toshiharu Shikanai [Japon]Source :
- The Plant Cell [ 1040-4651 ] ; 2009.
Abstract
In higher plants, the chloroplast NAD(P)H dehydrogenase (NDH) complex mediates photosystem I (PSI) cyclic and chlororespiratory electron transport. We reported previously that NDH interacts with the PSI complex to form a supercomplex (NDH-PSI). In this study, NDH18 and FKBP16-2 (FK506 Binding Protein 16-2), detected in the NDH-PSI supercomplex by mass spectrometry, were shown to be NDH subunits by the analysis of their knockdown lines. On the basis of extensive mutant characterization, we propose a structural model for chloroplast NDH, whereby NDH is divided into four subcomplexes. The subcomplex A and membrane subcomplex are conserved in cyanobacteria, but the subcomplex B and lumen subcomplex are specific to chloroplasts. Two minor light-harvesting complex I proteins, Lhca5 and Lhca6, were required for the full-size NDH-PSI supercomplex formation. Similar to
Url:
DOI: 10.1105/tpc.109.068791
PubMed: 19903870
PubMed Central: 2798312
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<author><name sortKey="Peng, Lianwei" sort="Peng, Lianwei" uniqKey="Peng L" first="Lianwei" last="Peng">Lianwei Peng</name>
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<series><title level="j">The Plant Cell</title>
<idno type="ISSN">1040-4651</idno>
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<imprint><date when="2009">2009</date>
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<front><div type="abstract" xml:lang="en"><p>In higher plants, the chloroplast NAD(P)H dehydrogenase (NDH) complex mediates photosystem I (PSI) cyclic and chlororespiratory electron transport. We reported previously that NDH interacts with the PSI complex to form a supercomplex (NDH-PSI). In this study, NDH18 and FKBP16-2 (FK506 Binding Protein 16-2), detected in the NDH-PSI supercomplex by mass spectrometry, were shown to be NDH subunits by the analysis of their knockdown lines. On the basis of extensive mutant characterization, we propose a structural model for chloroplast NDH, whereby NDH is divided into four subcomplexes. The subcomplex A and membrane subcomplex are conserved in cyanobacteria, but the subcomplex B and lumen subcomplex are specific to chloroplasts. Two minor light-harvesting complex I proteins, Lhca5 and Lhca6, were required for the full-size NDH-PSI supercomplex formation. Similar to <italic>crr pgr5</italic>
double mutants that completely lack cyclic electron flow activity around PSI, the <italic>lhca6 pgr5</italic>
double mutant exhibited a severe defect in growth. Consistent with the impaired NDH activity, photosynthesis was also severely affected in mature leaves of <italic>lhca6 pgr5</italic>
. We conclude that chloroplast NDH became equipped with the novel subcomplexes and became associated with PSI during the evolution of land plants, and this process may have facilitated the efficient operation of NDH.</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">plntcell</journal-id>
<journal-title-group><journal-title>The Plant Cell</journal-title>
</journal-title-group>
<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">19903870</article-id>
<article-id pub-id-type="pmc">2798312</article-id>
<article-id pub-id-type="publisher-id">068791</article-id>
<article-id pub-id-type="doi">10.1105/tpc.109.068791</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Research Articles</subject>
</subj-group>
</article-categories>
<title-group><article-title>Efficient Operation of NAD(P)H Dehydrogenase Requires Supercomplex Formation with Photosystem I via Minor LHCI in <italic>Arabidopsis</italic>
<xref ref-type="fn" rid="fn1">[W]</xref>
</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Peng</surname>
<given-names>Lianwei</given-names>
</name>
<xref ref-type="aff" rid="aff1">a</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Fukao</surname>
<given-names>Yoichiro</given-names>
</name>
<xref ref-type="aff" rid="aff2">b</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Fujiwara</surname>
<given-names>Masayuki</given-names>
</name>
<xref ref-type="aff" rid="aff2">b</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Takami</surname>
<given-names>Tsuneaki</given-names>
</name>
<xref ref-type="aff" rid="aff3">c</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Shikanai</surname>
<given-names>Toshiharu</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>
Department of Botany, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan</aff>
<aff id="aff2"><label>b</label>
Plant Science Education Unit, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Takayama, Ikoma, Nara 630-0101, Japan</aff>
<aff id="aff3"><label>c</label>
Graduate School of Agriculture, Kyushu University, Higashi-ku, Fukuoka 812-8581, Japan</aff>
<author-notes><corresp id="cor1"><label>1</label>
Address correspondence to <email>shikanai@pmg.bot.kyoto-u.ac.jp</email>
.</corresp>
</author-notes>
<pub-date pub-type="ppub"><month>11</month>
<year>2009</year>
</pub-date>
<volume>21</volume>
<issue>11</issue>
<fpage>3623</fpage>
<lpage>3640</lpage>
<history><date date-type="received"><day>19</day>
<month>5</month>
<year>2009</year>
</date>
<date date-type="rev-recd"><day>1</day>
<month>10</month>
<year>2009</year>
</date>
<date date-type="accepted"><day>23</day>
<month>10</month>
<year>2009</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2009, American Society of Plant Biologists</copyright-statement>
<copyright-year>2009</copyright-year>
</permissions>
<abstract><p>In higher plants, the chloroplast NAD(P)H dehydrogenase (NDH) complex mediates photosystem I (PSI) cyclic and chlororespiratory electron transport. We reported previously that NDH interacts with the PSI complex to form a supercomplex (NDH-PSI). In this study, NDH18 and FKBP16-2 (FK506 Binding Protein 16-2), detected in the NDH-PSI supercomplex by mass spectrometry, were shown to be NDH subunits by the analysis of their knockdown lines. On the basis of extensive mutant characterization, we propose a structural model for chloroplast NDH, whereby NDH is divided into four subcomplexes. The subcomplex A and membrane subcomplex are conserved in cyanobacteria, but the subcomplex B and lumen subcomplex are specific to chloroplasts. Two minor light-harvesting complex I proteins, Lhca5 and Lhca6, were required for the full-size NDH-PSI supercomplex formation. Similar to <italic>crr pgr5</italic>
double mutants that completely lack cyclic electron flow activity around PSI, the <italic>lhca6 pgr5</italic>
double mutant exhibited a severe defect in growth. Consistent with the impaired NDH activity, photosynthesis was also severely affected in mature leaves of <italic>lhca6 pgr5</italic>
. We conclude that chloroplast NDH became equipped with the novel subcomplexes and became associated with PSI during the evolution of land plants, and this process may have facilitated the efficient operation of NDH.</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: Toshiharu Shikanai (<email>shikanai@pmg.bot.kyoto-u.ac.jp</email>
).</p>
</fn>
<fn id="fn1"><label>[W]</label>
<p>Online version contains Web-only data.</p>
</fn>
<fn><p><ext-link ext-link-type="uri" xlink:href="www.plantcell.org/cgi/doi/10.1105/tpc.109.068791">www.plantcell.org/cgi/doi/10.1105/tpc.109.068791</ext-link>
</p>
</fn>
</fn-group>
</notes>
</front>
</pmc>
</record>
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