Characterization of the cinnamoyl-CoA reductase (CCR) gene family in Populus tomentosa reveals the enzymatic active sites and evolution of CCR.
Identifieur interne : 001483 ( Main/Exploration ); précédent : 001482; suivant : 001484Characterization of the cinnamoyl-CoA reductase (CCR) gene family in Populus tomentosa reveals the enzymatic active sites and evolution of CCR.
Auteurs : Nan Chao [République populaire de Chine] ; Ning Li [République populaire de Chine] ; Qi Qi [République populaire de Chine] ; Shuang Li [République populaire de Chine] ; Tong Lv [République populaire de Chine] ; Xiang-Ning Jiang [République populaire de Chine] ; Ying Gai [République populaire de Chine]Source :
- Planta [ 1432-2048 ] ; 2017.
Descripteurs français
- KwdFr :
- Aldehyde oxidoreductases (composition chimique), Aldehyde oxidoreductases (génétique), Alignement de séquences (MeSH), Chromosomes de plante (génétique), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Domaine catalytique (MeSH), Dosages enzymatiques (MeSH), Duplication de gène (MeSH), Famille multigénique (MeSH), Gènes de plante (MeSH), Mutagenèse dirigée (MeSH), Phylogenèse (MeSH), Populus (enzymologie), Populus (génétique), Protéines mutantes (composition chimique), Protéines recombinantes (métabolisme), Simulation de docking moléculaire (MeSH), Séquence conservée (génétique), Séquence d'acides aminés (MeSH), Température (MeSH), Évolution moléculaire (MeSH).
- MESH :
- composition chimique : Aldehyde oxidoreductases, Protéines mutantes.
- enzymologie : Populus.
- génétique : Aldehyde oxidoreductases, Chromosomes de plante, Populus, Séquence conservée.
- métabolisme : Protéines recombinantes.
- Alignement de séquences, Cinétique, Concentration en ions d'hydrogène, Domaine catalytique, Dosages enzymatiques, Duplication de gène, Famille multigénique, Gènes de plante, Mutagenèse dirigée, Phylogenèse, Simulation de docking moléculaire, Séquence d'acides aminés, Température, Évolution moléculaire.
English descriptors
- KwdEn :
- Aldehyde Oxidoreductases (chemistry), Aldehyde Oxidoreductases (genetics), Amino Acid Sequence (MeSH), Catalytic Domain (MeSH), Chromosomes, Plant (genetics), Conserved Sequence (genetics), Enzyme Assays (MeSH), Evolution, Molecular (MeSH), Gene Duplication (MeSH), Genes, Plant (MeSH), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), Molecular Docking Simulation (MeSH), Multigene Family (MeSH), Mutagenesis, Site-Directed (MeSH), Mutant Proteins (chemistry), Phylogeny (MeSH), Populus (enzymology), Populus (genetics), Recombinant Proteins (metabolism), Sequence Alignment (MeSH), Temperature (MeSH).
- MESH :
- chemical , chemistry : Aldehyde Oxidoreductases, Mutant Proteins.
- chemical , genetics : Aldehyde Oxidoreductases.
- enzymology : Populus.
- genetics : Chromosomes, Plant, Conserved Sequence, Populus.
- chemical , metabolism : Recombinant Proteins.
- Amino Acid Sequence, Catalytic Domain, Enzyme Assays, Evolution, Molecular, Gene Duplication, Genes, Plant, Hydrogen-Ion Concentration, Kinetics, Molecular Docking Simulation, Multigene Family, Mutagenesis, Site-Directed, Phylogeny, Sequence Alignment, Temperature.
Abstract
MAIN CONCLUSION
Two distinct cinnamoyl-coenzyme A reductases (CCRs) from Populus tomentosa were cloned and studied and active sites in CCRs were further identified based on sequence divergence, molecular simulation, and site-directed mutants. Cinnamoyl-coenzyme A (CoA) reductase (CCR) is the first committed gene in the lignin-specific pathway and plays a role in the lignin biosynthesis pathway. In this study, we cloned 11 genes encoding CCR or CCR-like proteins in Populus tomentosa. An enzymatic assay of the purified recombinant P. tomentosa (Pto) CCR and PtoCCR-like proteins indicated that only PtoCCR1 and PtoCCR7 had detectable activities toward hydroxycinnamoyl-CoA esters. PtoCCR1 exhibited specificity for feruloyl-CoA, with no detectable activity for any other hydroxycinnamoyl-CoA esters. However, PtoCCR7 catalyzed p-coumaroyl-CoA, caffeoyl-CoA, feruloyl-CoA, and sinapoyl-CoA with a preference for feruloyl-CoA. Site-directed mutations of selected amino acids divergent between PtoCCR1 and 7, combined with modeling and docking, showed that A132 in CCR7 combined with the catalytic triad might comprise the catalytic center. In CCR7, L192, F155, and H208 were identified as the substrate-binding sites, and site-directed mutations of these amino acids showed obvious changes in catalytic efficiency with respect to both feruloyl-CoA and sinapoyl-CoA. Mutant F155Y exhibited greater catalytic efficiency for sinapoyl-CoA compared with that of wild-type PtoCCR7. Finally, recent genome duplication events provided the foundation for CCR divergence. This study further identified the active sites in CCRs and the evolutionary process of CCRs in terrestrial plants.
DOI: 10.1007/s00425-016-2591-6
PubMed: 27580618
Affiliations:
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Le document en format XML
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xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083</wicri:regionArea><wicri:noRegion>100083</wicri:noRegion></affiliation></author><author><name sortKey="Li, Ning" sort="Li, Ning" uniqKey="Li N" first="Ning" last="Li">Ning Li</name><affiliation wicri:level="1"><nlm:affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083</wicri:regionArea><wicri:noRegion>100083</wicri:noRegion></affiliation></author><author><name sortKey="Qi, Qi" sort="Qi, Qi" uniqKey="Qi Q" first="Qi" last="Qi">Qi Qi</name><affiliation wicri:level="1"><nlm:affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083</wicri:regionArea><wicri:noRegion>100083</wicri:noRegion></affiliation></author><author><name sortKey="Li, Shuang" sort="Li, Shuang" uniqKey="Li S" first="Shuang" last="Li">Shuang Li</name><affiliation wicri:level="1"><nlm:affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083</wicri:regionArea><wicri:noRegion>100083</wicri:noRegion></affiliation></author><author><name sortKey="Lv, Tong" sort="Lv, Tong" uniqKey="Lv T" first="Tong" last="Lv">Tong Lv</name><affiliation wicri:level="1"><nlm:affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083</wicri:regionArea><wicri:noRegion>100083</wicri:noRegion></affiliation></author><author><name sortKey="Jiang, Xiang Ning" sort="Jiang, Xiang Ning" uniqKey="Jiang X" first="Xiang-Ning" last="Jiang">Xiang-Ning Jiang</name><affiliation wicri:level="1"><nlm:affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083</wicri:regionArea><wicri:noRegion>100083</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>The Tree and Ornamental Plant Breeding and Biotechnology Laboratory of Chinese Forestry Administration, Beijing, 100083, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>The Tree and Ornamental Plant Breeding and Biotechnology Laboratory of Chinese Forestry Administration, Beijing, 100083</wicri:regionArea><wicri:noRegion>100083</wicri:noRegion></affiliation></author><author><name sortKey="Gai, Ying" sort="Gai, Ying" uniqKey="Gai Y" first="Ying" last="Gai">Ying Gai</name><affiliation wicri:level="1"><nlm:affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China. gaiying@bjfu.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083</wicri:regionArea><wicri:noRegion>100083</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>The Tree and Ornamental Plant Breeding and Biotechnology Laboratory of Chinese Forestry Administration, Beijing, 100083, China. gaiying@bjfu.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>The Tree and Ornamental Plant Breeding and Biotechnology Laboratory of Chinese Forestry Administration, Beijing, 100083</wicri:regionArea><wicri:noRegion>100083</wicri:noRegion></affiliation></author></analytic><series><title level="j">Planta</title><idno type="eISSN">1432-2048</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aldehyde Oxidoreductases (chemistry)</term><term>Aldehyde Oxidoreductases (genetics)</term><term>Amino Acid Sequence (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Chromosomes, Plant (genetics)</term><term>Conserved Sequence (genetics)</term><term>Enzyme Assays (MeSH)</term><term>Evolution, Molecular (MeSH)</term><term>Gene Duplication (MeSH)</term><term>Genes, Plant (MeSH)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Kinetics (MeSH)</term><term>Molecular Docking Simulation (MeSH)</term><term>Multigene Family (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Mutant Proteins (chemistry)</term><term>Phylogeny (MeSH)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Sequence Alignment (MeSH)</term><term>Temperature (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aldehyde oxidoreductases (composition chimique)</term><term>Aldehyde oxidoreductases (génétique)</term><term>Alignement de séquences (MeSH)</term><term>Chromosomes de plante (génétique)</term><term>Cinétique (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Dosages enzymatiques (MeSH)</term><term>Duplication de gène (MeSH)</term><term>Famille multigénique (MeSH)</term><term>Gènes de plante (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Phylogenèse (MeSH)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Protéines mutantes (composition chimique)</term><term>Protéines recombinantes (métabolisme)</term><term>Simulation de docking moléculaire (MeSH)</term><term>Séquence conservée (génétique)</term><term>Séquence d'acides aminés (MeSH)</term><term>Température (MeSH)</term><term>Évolution moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Aldehyde Oxidoreductases</term><term>Mutant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Aldehyde Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Aldehyde oxidoreductases</term><term>Protéines mutantes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Chromosomes, Plant</term><term>Conserved Sequence</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Aldehyde oxidoreductases</term><term>Chromosomes de plante</term><term>Populus</term><term>Séquence conservée</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Catalytic Domain</term><term>Enzyme Assays</term><term>Evolution, Molecular</term><term>Gene Duplication</term><term>Genes, Plant</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Molecular Docking Simulation</term><term>Multigene Family</term><term>Mutagenesis, Site-Directed</term><term>Phylogeny</term><term>Sequence Alignment</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Domaine catalytique</term><term>Dosages enzymatiques</term><term>Duplication de gène</term><term>Famille multigénique</term><term>Gènes de plante</term><term>Mutagenèse dirigée</term><term>Phylogenèse</term><term>Simulation de docking moléculaire</term><term>Séquence d'acides aminés</term><term>Température</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>MAIN CONCLUSION</b></p><p>Two distinct cinnamoyl-coenzyme A reductases (CCRs) from Populus tomentosa were cloned and studied and active sites in CCRs were further identified based on sequence divergence, molecular simulation, and site-directed mutants. Cinnamoyl-coenzyme A (CoA) reductase (CCR) is the first committed gene in the lignin-specific pathway and plays a role in the lignin biosynthesis pathway. In this study, we cloned 11 genes encoding CCR or CCR-like proteins in Populus tomentosa. An enzymatic assay of the purified recombinant P. tomentosa (Pto) CCR and PtoCCR-like proteins indicated that only PtoCCR1 and PtoCCR7 had detectable activities toward hydroxycinnamoyl-CoA esters. PtoCCR1 exhibited specificity for feruloyl-CoA, with no detectable activity for any other hydroxycinnamoyl-CoA esters. However, PtoCCR7 catalyzed p-coumaroyl-CoA, caffeoyl-CoA, feruloyl-CoA, and sinapoyl-CoA with a preference for feruloyl-CoA. Site-directed mutations of selected amino acids divergent between PtoCCR1 and 7, combined with modeling and docking, showed that A132 in CCR7 combined with the catalytic triad might comprise the catalytic center. In CCR7, L192, F155, and H208 were identified as the substrate-binding sites, and site-directed mutations of these amino acids showed obvious changes in catalytic efficiency with respect to both feruloyl-CoA and sinapoyl-CoA. Mutant F155Y exhibited greater catalytic efficiency for sinapoyl-CoA compared with that of wild-type PtoCCR7. Finally, recent genome duplication events provided the foundation for CCR divergence. This study further identified the active sites in CCRs and the evolutionary process of CCRs in terrestrial plants.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27580618</PMID><DateCompleted><Year>2017</Year><Month>04</Month><Day>24</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-2048</ISSN><JournalIssue CitedMedium="Internet"><Volume>245</Volume><Issue>1</Issue><PubDate><Year>2017</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Planta</Title><ISOAbbreviation>Planta</ISOAbbreviation></Journal><ArticleTitle>Characterization of the cinnamoyl-CoA reductase (CCR) gene family in Populus tomentosa reveals the enzymatic active sites and evolution of CCR.</ArticleTitle><Pagination><MedlinePgn>61-75</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00425-016-2591-6</ELocationID><Abstract><AbstractText Label="MAIN CONCLUSION" NlmCategory="UNASSIGNED">Two distinct cinnamoyl-coenzyme A reductases (CCRs) from Populus tomentosa were cloned and studied and active sites in CCRs were further identified based on sequence divergence, molecular simulation, and site-directed mutants. Cinnamoyl-coenzyme A (CoA) reductase (CCR) is the first committed gene in the lignin-specific pathway and plays a role in the lignin biosynthesis pathway. In this study, we cloned 11 genes encoding CCR or CCR-like proteins in Populus tomentosa. An enzymatic assay of the purified recombinant P. tomentosa (Pto) CCR and PtoCCR-like proteins indicated that only PtoCCR1 and PtoCCR7 had detectable activities toward hydroxycinnamoyl-CoA esters. PtoCCR1 exhibited specificity for feruloyl-CoA, with no detectable activity for any other hydroxycinnamoyl-CoA esters. However, PtoCCR7 catalyzed p-coumaroyl-CoA, caffeoyl-CoA, feruloyl-CoA, and sinapoyl-CoA with a preference for feruloyl-CoA. Site-directed mutations of selected amino acids divergent between PtoCCR1 and 7, combined with modeling and docking, showed that A132 in CCR7 combined with the catalytic triad might comprise the catalytic center. In CCR7, L192, F155, and H208 were identified as the substrate-binding sites, and site-directed mutations of these amino acids showed obvious changes in catalytic efficiency with respect to both feruloyl-CoA and sinapoyl-CoA. Mutant F155Y exhibited greater catalytic efficiency for sinapoyl-CoA compared with that of wild-type PtoCCR7. Finally, recent genome duplication events provided the foundation for CCR divergence. This study further identified the active sites in CCRs and the evolutionary process of CCRs in terrestrial plants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chao</LastName><ForeName>Nan</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Ning</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Qi</LastName><ForeName>Qi</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Shuang</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lv</LastName><ForeName>Tong</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jiang</LastName><ForeName>Xiang-Ning</ForeName><Initials>XN</Initials><AffiliationInfo><Affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>The Tree and Ornamental Plant Breeding and Biotechnology Laboratory of Chinese Forestry Administration, Beijing, 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gai</LastName><ForeName>Ying</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, 100083, China. gaiying@bjfu.edu.cn.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>The Tree and Ornamental Plant Breeding and Biotechnology Laboratory of Chinese Forestry Administration, Beijing, 100083, China. gaiying@bjfu.edu.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>08</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Planta</MedlineTA><NlmUniqueID>1250576</NlmUniqueID><ISSNLinking>0032-0935</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050505">Mutant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.2.-</RegistryNumber><NameOfSubstance UI="D000445">Aldehyde Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.2.1.44</RegistryNumber><NameOfSubstance UI="C019904">cinnamoyl CoA reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000445" MajorTopicYN="N">Aldehyde Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="Y">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032461" MajorTopicYN="N">Chromosomes, Plant</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057075" MajorTopicYN="N">Enzyme Assays</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019143" MajorTopicYN="Y">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020440" MajorTopicYN="N">Gene Duplication</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017343" MajorTopicYN="N">Genes, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Binding sites</Keyword><Keyword MajorTopicYN="Y">Cinnamoyl-coenzyme A reductase</Keyword><Keyword MajorTopicYN="Y">Gene family</Keyword><Keyword MajorTopicYN="Y">Populus tomentosa</Keyword><Keyword MajorTopicYN="Y">Site-directed mutations</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>07</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>08</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>9</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Chao</name></noRegion><name sortKey="Gai, Ying" sort="Gai, Ying" uniqKey="Gai Y" first="Ying" last="Gai">Ying Gai</name><name sortKey="Gai, Ying" sort="Gai, Ying" uniqKey="Gai Y" first="Ying" last="Gai">Ying Gai</name><name sortKey="Jiang, Xiang Ning" sort="Jiang, Xiang Ning" uniqKey="Jiang X" first="Xiang-Ning" last="Jiang">Xiang-Ning Jiang</name><name sortKey="Jiang, Xiang Ning" sort="Jiang, Xiang Ning" uniqKey="Jiang X" first="Xiang-Ning" last="Jiang">Xiang-Ning Jiang</name><name sortKey="Li, Ning" sort="Li, Ning" uniqKey="Li N" first="Ning" last="Li">Ning Li</name><name sortKey="Li, Shuang" sort="Li, Shuang" uniqKey="Li S" first="Shuang" last="Li">Shuang Li</name><name sortKey="Lv, Tong" sort="Lv, Tong" uniqKey="Lv T" first="Tong" last="Lv">Tong Lv</name><name sortKey="Qi, Qi" sort="Qi, Qi" uniqKey="Qi Q" first="Qi" last="Qi">Qi Qi</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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