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CAD1 and CCR2 protein complex formation in monolignol biosynthesis in Populus trichocarpa.

Identifieur interne : 000A98 ( Main/Exploration ); précédent : 000A97; suivant : 000A99

CAD1 and CCR2 protein complex formation in monolignol biosynthesis in Populus trichocarpa.

Auteurs : Xiaojing Yan [République populaire de Chine] ; Jie Liu [États-Unis] ; Hoon Kim [États-Unis] ; Baoguang Liu [République populaire de Chine] ; Xiong Huang [République populaire de Chine] ; Zhichang Yang [États-Unis] ; Ying-Chung Jimmy Lin [République populaire de Chine, Taïwan] ; Hao Chen [États-Unis] ; Chenmin Yang [États-Unis] ; Jack P. Wang [États-Unis, République populaire de Chine] ; David C. Muddiman [États-Unis] ; John Ralph [États-Unis] ; Ronald R. Sederoff [États-Unis] ; Quanzi Li [République populaire de Chine] ; Vincent L. Chiang [États-Unis, République populaire de Chine]

Source :

RBID : pubmed:30276825

Descripteurs français

English descriptors

Abstract

Lignin is the major phenolic polymer in plant secondary cell walls and is polymerized from monomeric subunits, the monolignols. Eleven enzyme families are implicated in monolignol biosynthesis. Here, we studied the functions of members of the cinnamyl alcohol dehydrogenase (CAD) and cinnamoyl-CoA reductase (CCR) families in wood formation in Populus trichocarpa, including the regulatory effects of their transcripts and protein activities on monolignol biosynthesis. Enzyme activity assays from stem-differentiating xylem (SDX) proteins showed that RNAi suppression of PtrCAD1 in P. trichocarpa transgenics caused a reduction in SDX CCR activity. RNAi suppression of PtrCCR2, the only CCR member highly expressed in SDX, caused a reciprocal reduction in SDX protein CAD activities. The enzyme assays of mixed and coexpressed recombinant proteins supported physical interactions between PtrCAD1 and PtrCCR2. Biomolecular fluorescence complementation and pull-down/co-immunoprecipitation experiments supported a hypothesis of PtrCAD1/PtrCCR2 heterodimer formation. These results provide evidence for the formation of PtrCAD1/PtrCCR2 protein complexes in monolignol biosynthesis in planta.

DOI: 10.1111/nph.15505
PubMed: 30276825


Affiliations:


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Le document en format XML

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<name sortKey="Liu, Jie" sort="Liu, Jie" uniqKey="Liu J" first="Jie" last="Liu">Jie Liu</name>
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<nlm:affiliation>Department of Biochemistry and DOE Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, WI, 53726, USA.</nlm:affiliation>
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<nlm:affiliation>Department of Forestry, Beihua University, Jilin, 132013, China.</nlm:affiliation>
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<name sortKey="Lin, Ying Chung Jimmy" sort="Lin, Ying Chung Jimmy" uniqKey="Lin Y" first="Ying-Chung Jimmy" last="Lin">Ying-Chung Jimmy Lin</name>
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<name sortKey="Yang, Chenmin" sort="Yang, Chenmin" uniqKey="Yang C" first="Chenmin" last="Yang">Chenmin Yang</name>
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<name sortKey="Wang, Jack P" sort="Wang, Jack P" uniqKey="Wang J" first="Jack P" last="Wang">Jack P. Wang</name>
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<name sortKey="Ralph, John" sort="Ralph, John" uniqKey="Ralph J" first="John" last="Ralph">John Ralph</name>
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<nlm:affiliation>Department of Biochemistry and DOE Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, WI, 53726, USA.</nlm:affiliation>
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<wicri:regionArea>Department of Biochemistry and DOE Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, WI, 53726</wicri:regionArea>
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<nlm:affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC, 27695, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC, 27695</wicri:regionArea>
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<name sortKey="Li, Quanzi" sort="Li, Quanzi" uniqKey="Li Q" first="Quanzi" last="Li">Quanzi Li</name>
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<nlm:affiliation>State Key Laboratory of Tree Genetics and Breeding, Chinese Academy of Forestry, Beijing, 100091, China.</nlm:affiliation>
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<title level="j">The New phytologist</title>
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<term>Aldehyde Oxidoreductases (genetics)</term>
<term>Aldehyde Oxidoreductases (metabolism)</term>
<term>Down-Regulation (genetics)</term>
<term>Gene Expression Regulation, Plant (MeSH)</term>
<term>Lignin (metabolism)</term>
<term>Magnetic Resonance Spectroscopy (MeSH)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Plants, Genetically Modified (MeSH)</term>
<term>Populus (genetics)</term>
<term>Populus (metabolism)</term>
<term>RNA Interference (MeSH)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Xylem (metabolism)</term>
</keywords>
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<term>Aldehyde oxidoreductases (génétique)</term>
<term>Aldehyde oxidoreductases (métabolisme)</term>
<term>Interférence par ARN (MeSH)</term>
<term>Lignine (métabolisme)</term>
<term>Populus (génétique)</term>
<term>Populus (métabolisme)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Régulation de l'expression des gènes végétaux (MeSH)</term>
<term>Régulation négative (génétique)</term>
<term>Spectroscopie par résonance magnétique (MeSH)</term>
<term>Végétaux génétiquement modifiés (MeSH)</term>
<term>Xylème (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en">
<term>Aldehyde Oxidoreductases</term>
<term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Aldehyde Oxidoreductases</term>
<term>Lignin</term>
<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Down-Regulation</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Aldehyde oxidoreductases</term>
<term>Populus</term>
<term>Protéines végétales</term>
<term>Régulation négative</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Populus</term>
<term>Xylem</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Aldehyde oxidoreductases</term>
<term>Lignine</term>
<term>Populus</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
<term>Xylème</term>
</keywords>
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<term>Gene Expression Regulation, Plant</term>
<term>Magnetic Resonance Spectroscopy</term>
<term>Plants, Genetically Modified</term>
<term>RNA Interference</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr">
<term>Interférence par ARN</term>
<term>Régulation de l'expression des gènes végétaux</term>
<term>Spectroscopie par résonance magnétique</term>
<term>Végétaux génétiquement modifiés</term>
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<div type="abstract" xml:lang="en">Lignin is the major phenolic polymer in plant secondary cell walls and is polymerized from monomeric subunits, the monolignols. Eleven enzyme families are implicated in monolignol biosynthesis. Here, we studied the functions of members of the cinnamyl alcohol dehydrogenase (CAD) and cinnamoyl-CoA reductase (CCR) families in wood formation in Populus trichocarpa, including the regulatory effects of their transcripts and protein activities on monolignol biosynthesis. Enzyme activity assays from stem-differentiating xylem (SDX) proteins showed that RNAi suppression of PtrCAD1 in P. trichocarpa transgenics caused a reduction in SDX CCR activity. RNAi suppression of PtrCCR2, the only CCR member highly expressed in SDX, caused a reciprocal reduction in SDX protein CAD activities. The enzyme assays of mixed and coexpressed recombinant proteins supported physical interactions between PtrCAD1 and PtrCCR2. Biomolecular fluorescence complementation and pull-down/co-immunoprecipitation experiments supported a hypothesis of PtrCAD1/PtrCCR2 heterodimer formation. These results provide evidence for the formation of PtrCAD1/PtrCCR2 protein complexes in monolignol biosynthesis in planta.</div>
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<ArticleTitle>CAD1 and CCR2 protein complex formation in monolignol biosynthesis in Populus trichocarpa.</ArticleTitle>
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<AbstractText>Lignin is the major phenolic polymer in plant secondary cell walls and is polymerized from monomeric subunits, the monolignols. Eleven enzyme families are implicated in monolignol biosynthesis. Here, we studied the functions of members of the cinnamyl alcohol dehydrogenase (CAD) and cinnamoyl-CoA reductase (CCR) families in wood formation in Populus trichocarpa, including the regulatory effects of their transcripts and protein activities on monolignol biosynthesis. Enzyme activity assays from stem-differentiating xylem (SDX) proteins showed that RNAi suppression of PtrCAD1 in P. trichocarpa transgenics caused a reduction in SDX CCR activity. RNAi suppression of PtrCCR2, the only CCR member highly expressed in SDX, caused a reciprocal reduction in SDX protein CAD activities. The enzyme assays of mixed and coexpressed recombinant proteins supported physical interactions between PtrCAD1 and PtrCCR2. Biomolecular fluorescence complementation and pull-down/co-immunoprecipitation experiments supported a hypothesis of PtrCAD1/PtrCCR2 heterodimer formation. These results provide evidence for the formation of PtrCAD1/PtrCCR2 protein complexes in monolignol biosynthesis in planta.</AbstractText>
<CopyrightInformation>© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.</CopyrightInformation>
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<LastName>Yan</LastName>
<ForeName>Xiaojing</ForeName>
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<AffiliationInfo>
<Affiliation>State Key Laboratory of Tree Genetics and Breeding, Chinese Academy of Forestry, Beijing, 100091, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Research Institute of Forestry, Chinese Academy of Forestry, Beijing, 100091, China.</Affiliation>
</AffiliationInfo>
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<LastName>Liu</LastName>
<ForeName>Jie</ForeName>
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<LastName>Kim</LastName>
<ForeName>Hoon</ForeName>
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<Affiliation>Department of Biochemistry and DOE Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, WI, 53726, USA.</Affiliation>
</AffiliationInfo>
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<LastName>Liu</LastName>
<ForeName>Baoguang</ForeName>
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<Affiliation>State Key Laboratory of Tree Genetics and Breeding, Northeast Forestry University, Harbin, 150040, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Department of Forestry, Beihua University, Jilin, 132013, China.</Affiliation>
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<LastName>Ralph</LastName>
<ForeName>John</ForeName>
<Initials>J</Initials>
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</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Sederoff</LastName>
<ForeName>Ronald R</ForeName>
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<Grant>
<GrantID>CAFYBB2016ZX001-1</GrantID>
<Agency>Fundamental Research Funds of CAF</Agency>
<Country>International</Country>
</Grant>
<Grant>
<GrantID>2016YFD0600103</GrantID>
<Agency>National Key Research and Development Program of China</Agency>
<Country>International</Country>
</Grant>
<Grant>
<GrantID>DBI-0922391</GrantID>
<Agency>National Science Foundation Plant Genome Research Program Grant</Agency>
<Country>International</Country>
</Grant>
<Grant>
<GrantID>BER DE-FC02-07ER64494</GrantID>
<Agency>DOE Great Lakes Bioenergy Research Center</Agency>
<Country>International</Country>
</Grant>
<Grant>
<GrantID>DE-SC0018409</GrantID>
<Agency>DOE Great Lakes Bioenergy Research Center</Agency>
<Country>International</Country>
</Grant>
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<ArticleDate DateType="Electronic">
<Year>2018</Year>
<Month>10</Month>
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<Country>England</Country>
<MedlineTA>New Phytol</MedlineTA>
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