Functional redundancy of the two 5-hydroxylases in monolignol biosynthesis of Populus trichocarpa: LC-MS/MS based protein quantification and metabolic flux analysis.
Identifieur interne : 002A75 ( Main/Exploration ); précédent : 002A74; suivant : 002A76Functional redundancy of the two 5-hydroxylases in monolignol biosynthesis of Populus trichocarpa: LC-MS/MS based protein quantification and metabolic flux analysis.
Auteurs : Jack P. Wang [États-Unis] ; Christopher M. Shuford ; Quanzi Li ; Jina Song ; Ying-Chung Lin ; Ying-Hsuan Sun ; Hsi-Chuan Chen ; Cranos M. Williams ; David C. Muddiman ; Ronald R. Sederoff ; Vincent L. ChiangSource :
- Planta [ 1432-2048 ] ; 2012.
Descripteurs français
- KwdFr :
- Cinétique (MeSH), Clonage moléculaire (MeSH), Hydroxylation (MeSH), Levures (métabolisme), Lignine (analyse), Lignine (biosynthèse), Mixed function oxygenases (métabolisme), Populus (métabolisme), Régulation de l'expression des gènes codant pour des enzymes (MeSH), Régulation de l'expression des gènes végétaux (MeSH), Végétaux génétiquement modifiés (MeSH), Xylème (enzymologie).
- MESH :
- analyse : Lignine.
- biosynthèse : Lignine.
- enzymologie : Xylème.
- métabolisme : Levures, Mixed function oxygenases, Populus.
- Cinétique, Clonage moléculaire, Hydroxylation, Régulation de l'expression des gènes codant pour des enzymes, Régulation de l'expression des gènes végétaux, Végétaux génétiquement modifiés.
English descriptors
- KwdEn :
- Cloning, Molecular (MeSH), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Plant (MeSH), Hydroxylation (MeSH), Kinetics (MeSH), Lignin (analysis), Lignin (biosynthesis), Mixed Function Oxygenases (metabolism), Plants, Genetically Modified (MeSH), Populus (metabolism), Xylem (enzymology), Yeasts (metabolism).
- MESH :
- chemical , analysis : Lignin.
- chemical , biosynthesis : Lignin.
- chemical , metabolism : Mixed Function Oxygenases.
- enzymology : Xylem.
- metabolism : Populus, Yeasts.
- Cloning, Molecular, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Hydroxylation, Kinetics, Plants, Genetically Modified.
Abstract
Flowering plants have syringyl and guaiacyl subunits in lignin in contrast to the guaiacyl lignin in gymnosperms. The biosynthesis of syringyl subunits is initiated by coniferaldehyde 5-hydroxylase (CAld5H). In Populus trichocarpa there are two closely related CAld5H enzymes (PtrCAld5H1 and PtrCAld5H2) associated with lignin biosynthesis during wood formation. We used yeast recombinant PtrCAld5H1 and PtrCAld5H2 proteins to carry out Michaelis-Menten and inhibition kinetics with LC-MS/MS based absolute protein quantification. CAld5H, a monooxygenase, requires a cytochrome P450 reductase (CPR) as an electron donor. We cloned and expressed three P. trichocarpa CPRs in yeast and show that all are active with both CAld5Hs. The kinetic analysis shows both CAld5Hs have essentially the same biochemical functions. When both CAld5Hs are coexpressed in the same yeast membranes, the resulting enzyme activities are additive, suggesting functional redundancy and independence of these two enzymes. Simulated reaction flux based on Michaelis-Menten kinetics and inhibition kinetics confirmed the redundancy and independence. Subcellular localization of both CAld5Hs as sGFP fusion proteins expressed in P. trichocarpa differentiating xylem protoplasts indicate that they are endoplasmic reticulum resident proteins. These results imply that during wood formation, 5-hydroxylation in monolignol biosynthesis of P. trichocarpa requires the combined metabolic flux of these two CAld5Hs to maintain adequate biosynthesis of syringyl lignin. The combination of genetic analysis, absolute protein quantitation-based enzyme kinetics, homologous CPR specificity, SNP characterization, and ER localization provides a more rigorous basis for a comprehensive systems understanding of 5-hydroxylation in lignin biosynthesis.
DOI: 10.1007/s00425-012-1663-5
PubMed: 22628084
Affiliations:
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Le document en format XML
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Wang</name><affiliation wicri:level="2"><nlm:affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695, USA. jpwang@ncsu.edu</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><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author><author><name sortKey="Shuford, Christopher M" sort="Shuford, Christopher M" uniqKey="Shuford C" first="Christopher M" last="Shuford">Christopher M. 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Wang</name><affiliation wicri:level="2"><nlm:affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695, USA. jpwang@ncsu.edu</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><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author><author><name sortKey="Shuford, Christopher M" sort="Shuford, Christopher M" uniqKey="Shuford C" first="Christopher M" last="Shuford">Christopher M. Shuford</name></author><author><name sortKey="Li, Quanzi" sort="Li, Quanzi" uniqKey="Li Q" first="Quanzi" last="Li">Quanzi Li</name></author><author><name sortKey="Song, Jina" sort="Song, Jina" uniqKey="Song J" first="Jina" last="Song">Jina Song</name></author><author><name sortKey="Lin, Ying Chung" sort="Lin, Ying Chung" uniqKey="Lin Y" first="Ying-Chung" last="Lin">Ying-Chung Lin</name></author><author><name sortKey="Sun, Ying Hsuan" sort="Sun, Ying Hsuan" uniqKey="Sun Y" first="Ying-Hsuan" last="Sun">Ying-Hsuan Sun</name></author><author><name sortKey="Chen, Hsi Chuan" sort="Chen, Hsi Chuan" uniqKey="Chen H" first="Hsi-Chuan" last="Chen">Hsi-Chuan Chen</name></author><author><name sortKey="Williams, Cranos M" sort="Williams, Cranos M" uniqKey="Williams C" first="Cranos M" last="Williams">Cranos M. Williams</name></author><author><name sortKey="Muddiman, David C" sort="Muddiman, David C" uniqKey="Muddiman D" first="David C" last="Muddiman">David C. Muddiman</name></author><author><name sortKey="Sederoff, Ronald R" sort="Sederoff, Ronald R" uniqKey="Sederoff R" first="Ronald R" last="Sederoff">Ronald R. Sederoff</name></author><author><name sortKey="Chiang, Vincent L" sort="Chiang, Vincent L" uniqKey="Chiang V" first="Vincent L" last="Chiang">Vincent L. Chiang</name></author></analytic><series><title level="j">Planta</title><idno type="eISSN">1432-2048</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cloning, Molecular (MeSH)</term><term>Gene Expression Regulation, Enzymologic (MeSH)</term><term>Gene Expression Regulation, Plant (MeSH)</term><term>Hydroxylation (MeSH)</term><term>Kinetics (MeSH)</term><term>Lignin (analysis)</term><term>Lignin (biosynthesis)</term><term>Mixed Function Oxygenases (metabolism)</term><term>Plants, Genetically Modified (MeSH)</term><term>Populus (metabolism)</term><term>Xylem (enzymology)</term><term>Yeasts (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Hydroxylation (MeSH)</term><term>Levures (métabolisme)</term><term>Lignine (analyse)</term><term>Lignine (biosynthèse)</term><term>Mixed function oxygenases (métabolisme)</term><term>Populus (métabolisme)</term><term>Régulation de l'expression des gènes codant pour des enzymes (MeSH)</term><term>Régulation de l'expression des gènes végétaux (MeSH)</term><term>Végétaux génétiquement modifiés (MeSH)</term><term>Xylème (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Mixed Function Oxygenases</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Xylème</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Xylem</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Populus</term><term>Yeasts</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Levures</term><term>Mixed function oxygenases</term><term>Populus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Gene Expression Regulation, Enzymologic</term><term>Gene Expression Regulation, Plant</term><term>Hydroxylation</term><term>Kinetics</term><term>Plants, Genetically Modified</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Clonage moléculaire</term><term>Hydroxylation</term><term>Régulation de l'expression des gènes codant pour des enzymes</term><term>Régulation de l'expression des gènes végétaux</term><term>Végétaux génétiquement modifiés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Flowering plants have syringyl and guaiacyl subunits in lignin in contrast to the guaiacyl lignin in gymnosperms. The biosynthesis of syringyl subunits is initiated by coniferaldehyde 5-hydroxylase (CAld5H). In Populus trichocarpa there are two closely related CAld5H enzymes (PtrCAld5H1 and PtrCAld5H2) associated with lignin biosynthesis during wood formation. We used yeast recombinant PtrCAld5H1 and PtrCAld5H2 proteins to carry out Michaelis-Menten and inhibition kinetics with LC-MS/MS based absolute protein quantification. CAld5H, a monooxygenase, requires a cytochrome P450 reductase (CPR) as an electron donor. We cloned and expressed three P. trichocarpa CPRs in yeast and show that all are active with both CAld5Hs. The kinetic analysis shows both CAld5Hs have essentially the same biochemical functions. When both CAld5Hs are coexpressed in the same yeast membranes, the resulting enzyme activities are additive, suggesting functional redundancy and independence of these two enzymes. Simulated reaction flux based on Michaelis-Menten kinetics and inhibition kinetics confirmed the redundancy and independence. Subcellular localization of both CAld5Hs as sGFP fusion proteins expressed in P. trichocarpa differentiating xylem protoplasts indicate that they are endoplasmic reticulum resident proteins. These results imply that during wood formation, 5-hydroxylation in monolignol biosynthesis of P. trichocarpa requires the combined metabolic flux of these two CAld5Hs to maintain adequate biosynthesis of syringyl lignin. The combination of genetic analysis, absolute protein quantitation-based enzyme kinetics, homologous CPR specificity, SNP characterization, and ER localization provides a more rigorous basis for a comprehensive systems understanding of 5-hydroxylation in lignin biosynthesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22628084</PMID><DateCompleted><Year>2013</Year><Month>03</Month><Day>26</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>236</Volume><Issue>3</Issue><PubDate><Year>2012</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Planta</Title><ISOAbbreviation>Planta</ISOAbbreviation></Journal><ArticleTitle>Functional redundancy of the two 5-hydroxylases in monolignol biosynthesis of Populus trichocarpa: LC-MS/MS based protein quantification and metabolic flux analysis.</ArticleTitle><Pagination><MedlinePgn>795-808</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00425-012-1663-5</ELocationID><Abstract><AbstractText>Flowering plants have syringyl and guaiacyl subunits in lignin in contrast to the guaiacyl lignin in gymnosperms. The biosynthesis of syringyl subunits is initiated by coniferaldehyde 5-hydroxylase (CAld5H). In Populus trichocarpa there are two closely related CAld5H enzymes (PtrCAld5H1 and PtrCAld5H2) associated with lignin biosynthesis during wood formation. We used yeast recombinant PtrCAld5H1 and PtrCAld5H2 proteins to carry out Michaelis-Menten and inhibition kinetics with LC-MS/MS based absolute protein quantification. CAld5H, a monooxygenase, requires a cytochrome P450 reductase (CPR) as an electron donor. We cloned and expressed three P. trichocarpa CPRs in yeast and show that all are active with both CAld5Hs. The kinetic analysis shows both CAld5Hs have essentially the same biochemical functions. When both CAld5Hs are coexpressed in the same yeast membranes, the resulting enzyme activities are additive, suggesting functional redundancy and independence of these two enzymes. Simulated reaction flux based on Michaelis-Menten kinetics and inhibition kinetics confirmed the redundancy and independence. Subcellular localization of both CAld5Hs as sGFP fusion proteins expressed in P. trichocarpa differentiating xylem protoplasts indicate that they are endoplasmic reticulum resident proteins. These results imply that during wood formation, 5-hydroxylation in monolignol biosynthesis of P. trichocarpa requires the combined metabolic flux of these two CAld5Hs to maintain adequate biosynthesis of syringyl lignin. The combination of genetic analysis, absolute protein quantitation-based enzyme kinetics, homologous CPR specificity, SNP characterization, and ER localization provides a more rigorous basis for a comprehensive systems understanding of 5-hydroxylation in lignin biosynthesis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Jack P</ForeName><Initials>JP</Initials><AffiliationInfo><Affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695, USA. jpwang@ncsu.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shuford</LastName><ForeName>Christopher M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Quanzi</ForeName><Initials>Q</Initials></Author><Author ValidYN="Y"><LastName>Song</LastName><ForeName>Jina</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Ying-Chung</ForeName><Initials>YC</Initials></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Ying-Hsuan</ForeName><Initials>YH</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Hsi-Chuan</ForeName><Initials>HC</Initials></Author><Author ValidYN="Y"><LastName>Williams</LastName><ForeName>Cranos M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Muddiman</LastName><ForeName>David C</ForeName><Initials>DC</Initials></Author><Author ValidYN="Y"><LastName>Sederoff</LastName><ForeName>Ronald R</ForeName><Initials>RR</Initials></Author><Author ValidYN="Y"><LastName>Chiang</LastName><ForeName>Vincent L</ForeName><Initials>VL</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>05</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Planta</MedlineTA><NlmUniqueID>1250576</NlmUniqueID><ISSNLinking>0032-0935</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D006899">Mixed Function Oxygenases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015971" MajorTopicYN="N">Gene Expression Regulation, Enzymologic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006900" MajorTopicYN="N">Hydroxylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006899" MajorTopicYN="N">Mixed Function Oxygenases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D030821" MajorTopicYN="N">Plants, Genetically Modified</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D052584" MajorTopicYN="N">Xylem</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015003" MajorTopicYN="N">Yeasts</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>03</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>05</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>5</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>5</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>3</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22628084</ArticleId><ArticleId 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Chiang</name><name sortKey="Li, Quanzi" sort="Li, Quanzi" uniqKey="Li Q" first="Quanzi" last="Li">Quanzi Li</name><name sortKey="Lin, Ying Chung" sort="Lin, Ying Chung" uniqKey="Lin Y" first="Ying-Chung" last="Lin">Ying-Chung Lin</name><name sortKey="Muddiman, David C" sort="Muddiman, David C" uniqKey="Muddiman D" first="David C" last="Muddiman">David C. Muddiman</name><name sortKey="Sederoff, Ronald R" sort="Sederoff, Ronald R" uniqKey="Sederoff R" first="Ronald R" last="Sederoff">Ronald R. Sederoff</name><name sortKey="Shuford, Christopher M" sort="Shuford, Christopher M" uniqKey="Shuford C" first="Christopher M" last="Shuford">Christopher M. Shuford</name><name sortKey="Song, Jina" sort="Song, Jina" uniqKey="Song J" first="Jina" last="Song">Jina Song</name><name sortKey="Sun, Ying Hsuan" sort="Sun, Ying Hsuan" uniqKey="Sun Y" first="Ying-Hsuan" last="Sun">Ying-Hsuan Sun</name><name sortKey="Williams, Cranos M" sort="Williams, Cranos M" uniqKey="Williams C" first="Cranos M" last="Williams">Cranos M. Williams</name></noCountry><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Wang, Jack P" sort="Wang, Jack P" uniqKey="Wang J" first="Jack P" last="Wang">Jack P. Wang</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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