The plastid NAD(P)H dehydrogenase-like complex: structure, function and evolutionary dynamics.
Identifieur interne : 000095 ( Main/Corpus ); précédent : 000094; suivant : 000096The plastid NAD(P)H dehydrogenase-like complex: structure, function and evolutionary dynamics.
Auteurs : Deserah D. Strand ; Lucio D'Andrea ; Ralph BockSource :
- The Biochemical journal [ 1470-8728 ] ; 2019.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Photosystem I Protein Complex.
- chemical , metabolism : NADP, Photosystem I Protein Complex, Plastoquinone.
- metabolism : Plants, Thylakoids.
- Biological Evolution, Electron Transport, Oxidation-Reduction.
Abstract
The thylakoid NAD(P)H dehydrogenase-like (NDH) complex is a large protein complex that reduces plastoquinone and pumps protons into the lumen generating protonmotive force. In plants, the complex consists of both nuclear and chloroplast-encoded subunits. Despite its perceived importance for stress tolerance and ATP generation, chloroplast-encoded NDH subunits have been lost numerous times during evolution in species occupying seemingly unrelated environmental niches. We have generated a phylogenetic tree that reveals independent losses in multiple phylogenetic lineages, and we use this tree as a reference to discuss possible evolutionary contexts that may have relaxed selective pressure for retention of ndh genes. While we are still yet unable to pinpoint a singular specific lifestyle that negates the need for NDH, we are able to rule out several long-standing explanations. In light of this, we discuss the biochemical changes that would be required for the chloroplast to dispense with NDH functionality with regards to known and proposed NDH-related reactions.
DOI: 10.1042/BCJ20190365
PubMed: 31654059
Links to Exploration step
pubmed:31654059Le document en format XML
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<author><name sortKey="Strand, Deserah D" sort="Strand, Deserah D" uniqKey="Strand D" first="Deserah D" last="Strand">Deserah D. Strand</name>
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<author><name sortKey="D Andrea, Lucio" sort="D Andrea, Lucio" uniqKey="D Andrea L" first="Lucio" last="D'Andrea">Lucio D'Andrea</name>
<affiliation><nlm:affiliation>Max-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, D-14476 Potsdam-Golm, Germany.</nlm:affiliation>
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<author><name sortKey="Bock, Ralph" sort="Bock, Ralph" uniqKey="Bock R" first="Ralph" last="Bock">Ralph Bock</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">The plastid NAD(P)H dehydrogenase-like complex: structure, function and evolutionary dynamics.</title>
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<author><name sortKey="Bock, Ralph" sort="Bock, Ralph" uniqKey="Bock R" first="Ralph" last="Bock">Ralph Bock</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biological Evolution (MeSH)</term>
<term>Electron Transport (MeSH)</term>
<term>NADP (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Photosystem I Protein Complex (chemistry)</term>
<term>Photosystem I Protein Complex (metabolism)</term>
<term>Plants (metabolism)</term>
<term>Plastoquinone (metabolism)</term>
<term>Thylakoids (metabolism)</term>
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<term>Photosystem I Protein Complex</term>
<term>Plastoquinone</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plants</term>
<term>Thylakoids</term>
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<front><div type="abstract" xml:lang="en">The thylakoid NAD(P)H dehydrogenase-like (NDH) complex is a large protein complex that reduces plastoquinone and pumps protons into the lumen generating protonmotive force. In plants, the complex consists of both nuclear and chloroplast-encoded subunits. Despite its perceived importance for stress tolerance and ATP generation, chloroplast-encoded NDH subunits have been lost numerous times during evolution in species occupying seemingly unrelated environmental niches. We have generated a phylogenetic tree that reveals independent losses in multiple phylogenetic lineages, and we use this tree as a reference to discuss possible evolutionary contexts that may have relaxed selective pressure for retention of ndh genes. While we are still yet unable to pinpoint a singular specific lifestyle that negates the need for NDH, we are able to rule out several long-standing explanations. In light of this, we discuss the biochemical changes that would be required for the chloroplast to dispense with NDH functionality with regards to known and proposed NDH-related reactions.</div>
</front>
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<Month>10</Month>
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<Title>The Biochemical journal</Title>
<ISOAbbreviation>Biochem J</ISOAbbreviation>
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<ArticleTitle>The plastid NAD(P)H dehydrogenase-like complex: structure, function and evolutionary dynamics.</ArticleTitle>
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<Abstract><AbstractText>The thylakoid NAD(P)H dehydrogenase-like (NDH) complex is a large protein complex that reduces plastoquinone and pumps protons into the lumen generating protonmotive force. In plants, the complex consists of both nuclear and chloroplast-encoded subunits. Despite its perceived importance for stress tolerance and ATP generation, chloroplast-encoded NDH subunits have been lost numerous times during evolution in species occupying seemingly unrelated environmental niches. We have generated a phylogenetic tree that reveals independent losses in multiple phylogenetic lineages, and we use this tree as a reference to discuss possible evolutionary contexts that may have relaxed selective pressure for retention of ndh genes. While we are still yet unable to pinpoint a singular specific lifestyle that negates the need for NDH, we are able to rule out several long-standing explanations. In light of this, we discuss the biochemical changes that would be required for the chloroplast to dispense with NDH functionality with regards to known and proposed NDH-related reactions.</AbstractText>
<CopyrightInformation>© 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Strand</LastName>
<ForeName>Deserah D</ForeName>
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<MedlineTA>Biochem J</MedlineTA>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">NADPH dehydrogenase-like complex</Keyword>
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