PoplarV1, Main, Exploration, bibRecord, 002D96

Membrane protein complexes catalyze both 4- and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis.

Identifieur interne : 002D96 ( Main/Exploration ); précédent : 002D95; suivant : 002D97

Membrane protein complexes catalyze both 4- and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis.

Auteurs : Hsi-Chuan Chen [États-Unis] ; Quanzi Li ; Christopher M. Shuford ; Jie Liu ; David C. Muddiman ; Ronald R. Sederoff ; Vincent L. Chiang

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2011.

RBID : pubmed:22160716

Descripteurs français

English descriptors

KwdEn :
- Carboxylic Ester Hydrolases (chemistry), Carboxylic Ester Hydrolases (metabolism), Chromatography, Liquid (MeSH), DNA Primers (genetics), Hydroxylation (MeSH), Immunoprecipitation (MeSH), Kinetics (MeSH), Lignin (biosynthesis), Mass Spectrometry (MeSH), Membrane Proteins (chemistry), Membrane Proteins (metabolism), Microscopy, Confocal (MeSH), Molecular Structure (MeSH), Multiprotein Complexes (chemistry), Multiprotein Complexes (metabolism), Phenols (MeSH), Phenylpropionates (MeSH), Plasmids (genetics), Populus (metabolism), Propionates (MeSH), Trans-Cinnamate 4-Monooxygenase (chemistry), Trans-Cinnamate 4-Monooxygenase (metabolism), Xylem (metabolism), Yeasts (MeSH).
MESH :
- chemical , biosynthesis : Lignin.
- chemical , chemistry : Carboxylic Ester Hydrolases, Membrane Proteins, Multiprotein Complexes, Trans-Cinnamate 4-Monooxygenase.
- chemical , genetics : DNA Primers.
- chemical , metabolism : Carboxylic Ester Hydrolases, Membrane Proteins, Multiprotein Complexes, Trans-Cinnamate 4-Monooxygenase.
- genetics : Plasmids.
- metabolism : Populus, Xylem.
- Chromatography, Liquid, Hydroxylation, Immunoprecipitation, Kinetics, Mass Spectrometry, Microscopy, Confocal, Molecular Structure, Phenols, Phenylpropionates, Propionates, Yeasts.

Abstract

The hydroxylation of 4- and 3-ring carbons of cinnamic acid derivatives during monolignol biosynthesis are key steps that determine the structure and properties of lignin. Individual enzymes have been thought to catalyze these reactions. In stem differentiating xylem (SDX) of Populus trichocarpa, two cinnamic acid 4-hydroxylases (PtrC4H1 and PtrC4H2) and a p-coumaroyl ester 3-hydroxylase (PtrC3H3) are the enzymes involved in these reactions. Here we present evidence that these hydroxylases interact, forming heterodimeric (PtrC4H1/C4H2, PtrC4H1/C3H3, and PtrC4H2/C3H3) and heterotrimeric (PtrC4H1/C4H2/C3H3) membrane protein complexes. Enzyme kinetics using yeast recombinant proteins demonstrated that the enzymatic efficiency (V(max)/k(m)) for any of the complexes is 70-6,500 times greater than that of the individual proteins. The highest increase in efficiency was found for the PtrC4H1/C4H2/C3H3-mediated p-coumaroyl ester 3-hydroxylation. Affinity purification-quantitative mass spectrometry, bimolecular fluorescence complementation, chemical cross-linking, and reciprocal coimmunoprecipitation provide further evidence for these multiprotein complexes. The activities of the recombinant and SDX plant proteins demonstrate two protein-complex-mediated 3-hydroxylation paths in monolignol biosynthesis in P. trichocarpa SDX; one converts p-coumaric acid to caffeic acid and the other converts p-coumaroyl shikimic acid to caffeoyl shikimic acid. Cinnamic acid 4-hydroxylation is also mediated by the same protein complexes. These results provide direct evidence for functional involvement of membrane protein complexes in monolignol biosynthesis.

DOI: 10.1073/pnas.1116416109
PubMed: 22160716
PubMed Central: PMC3248547

Affiliations:

Links toward previous steps (curation, corpus...)

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to stream Main, to step Curation: 002C04

Le document en format XML

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<term>Carboxylic Ester Hydrolases (metabolism)</term>
<term>Chromatography, Liquid (MeSH)</term>
<term>DNA Primers (genetics)</term>
<term>Hydroxylation (MeSH)</term>
<term>Immunoprecipitation (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Lignin (biosynthesis)</term>
<term>Mass Spectrometry (MeSH)</term>
<term>Membrane Proteins (chemistry)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Microscopy, Confocal (MeSH)</term>
<term>Molecular Structure (MeSH)</term>
<term>Multiprotein Complexes (chemistry)</term>
<term>Multiprotein Complexes (metabolism)</term>
<term>Phenols (MeSH)</term>
<term>Phenylpropionates (MeSH)</term>
<term>Plasmids (genetics)</term>
<term>Populus (metabolism)</term>
<term>Propionates (MeSH)</term>
<term>Trans-Cinnamate 4-Monooxygenase (chemistry)</term>
<term>Trans-Cinnamate 4-Monooxygenase (metabolism)</term>
<term>Xylem (metabolism)</term>
<term>Yeasts (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN (génétique)</term>
<term>Carboxylic ester hydrolases (composition chimique)</term>
<term>Carboxylic ester hydrolases (métabolisme)</term>
<term>Chromatographie en phase liquide (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Complexes multiprotéiques (composition chimique)</term>
<term>Complexes multiprotéiques (métabolisme)</term>
<term>Hydroxylation (MeSH)</term>
<term>Immunoprécipitation (MeSH)</term>
<term>Levures (MeSH)</term>
<term>Lignine (biosynthèse)</term>
<term>Microscopie confocale (MeSH)</term>
<term>Phénols (MeSH)</term>
<term>Phénylpropionates (MeSH)</term>
<term>Plasmides (génétique)</term>
<term>Populus (métabolisme)</term>
<term>Propionates (MeSH)</term>
<term>Protéines membranaires (composition chimique)</term>
<term>Protéines membranaires (métabolisme)</term>
<term>Spectrométrie de masse (MeSH)</term>
<term>Structure moléculaire (MeSH)</term>
<term>Trans-cinnamate 4-monooxygenase (composition chimique)</term>
<term>Trans-cinnamate 4-monooxygenase (métabolisme)</term>
<term>Xylème (métabolisme)</term>
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<term>Membrane Proteins</term>
<term>Multiprotein Complexes</term>
<term>Trans-Cinnamate 4-Monooxygenase</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Carboxylic ester hydrolases</term>
<term>Complexes multiprotéiques</term>
<term>Protéines membranaires</term>
<term>Trans-cinnamate 4-monooxygenase</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Plasmids</term>
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<term>Xylem</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carboxylic ester hydrolases</term>
<term>Complexes multiprotéiques</term>
<term>Populus</term>
<term>Protéines membranaires</term>
<term>Trans-cinnamate 4-monooxygenase</term>
<term>Xylème</term>
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<keywords scheme="MESH" xml:lang="en"><term>Chromatography, Liquid</term>
<term>Hydroxylation</term>
<term>Immunoprecipitation</term>
<term>Kinetics</term>
<term>Mass Spectrometry</term>
<term>Microscopy, Confocal</term>
<term>Molecular Structure</term>
<term>Phenols</term>
<term>Phenylpropionates</term>
<term>Propionates</term>
<term>Yeasts</term>
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<term>Cinétique</term>
<term>Hydroxylation</term>
<term>Immunoprécipitation</term>
<term>Levures</term>
<term>Microscopie confocale</term>
<term>Phénols</term>
<term>Phénylpropionates</term>
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<front><div type="abstract" xml:lang="en">The hydroxylation of 4- and 3-ring carbons of cinnamic acid derivatives during monolignol biosynthesis are key steps that determine the structure and properties of lignin. Individual enzymes have been thought to catalyze these reactions. In stem differentiating xylem (SDX) of Populus trichocarpa, two cinnamic acid 4-hydroxylases (PtrC4H1 and PtrC4H2) and a p-coumaroyl ester 3-hydroxylase (PtrC3H3) are the enzymes involved in these reactions. Here we present evidence that these hydroxylases interact, forming heterodimeric (PtrC4H1/C4H2, PtrC4H1/C3H3, and PtrC4H2/C3H3) and heterotrimeric (PtrC4H1/C4H2/C3H3) membrane protein complexes. Enzyme kinetics using yeast recombinant proteins demonstrated that the enzymatic efficiency (V(max)/k(m)) for any of the complexes is 70-6,500 times greater than that of the individual proteins. The highest increase in efficiency was found for the PtrC4H1/C4H2/C3H3-mediated p-coumaroyl ester 3-hydroxylation. Affinity purification-quantitative mass spectrometry, bimolecular fluorescence complementation, chemical cross-linking, and reciprocal coimmunoprecipitation provide further evidence for these multiprotein complexes. The activities of the recombinant and SDX plant proteins demonstrate two protein-complex-mediated 3-hydroxylation paths in monolignol biosynthesis in P. trichocarpa SDX; one converts p-coumaric acid to caffeic acid and the other converts p-coumaroyl shikimic acid to caffeoyl shikimic acid. Cinnamic acid 4-hydroxylation is also mediated by the same protein complexes. These results provide direct evidence for functional involvement of membrane protein complexes in monolignol biosynthesis.</div>
</front>
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<ArticleTitle>Membrane protein complexes catalyze both 4- and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis.</ArticleTitle>
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<Abstract><AbstractText>The hydroxylation of 4- and 3-ring carbons of cinnamic acid derivatives during monolignol biosynthesis are key steps that determine the structure and properties of lignin. Individual enzymes have been thought to catalyze these reactions. In stem differentiating xylem (SDX) of Populus trichocarpa, two cinnamic acid 4-hydroxylases (PtrC4H1 and PtrC4H2) and a p-coumaroyl ester 3-hydroxylase (PtrC3H3) are the enzymes involved in these reactions. Here we present evidence that these hydroxylases interact, forming heterodimeric (PtrC4H1/C4H2, PtrC4H1/C3H3, and PtrC4H2/C3H3) and heterotrimeric (PtrC4H1/C4H2/C3H3) membrane protein complexes. Enzyme kinetics using yeast recombinant proteins demonstrated that the enzymatic efficiency (V(max)/k(m)) for any of the complexes is 70-6,500 times greater than that of the individual proteins. The highest increase in efficiency was found for the PtrC4H1/C4H2/C3H3-mediated p-coumaroyl ester 3-hydroxylation. Affinity purification-quantitative mass spectrometry, bimolecular fluorescence complementation, chemical cross-linking, and reciprocal coimmunoprecipitation provide further evidence for these multiprotein complexes. The activities of the recombinant and SDX plant proteins demonstrate two protein-complex-mediated 3-hydroxylation paths in monolignol biosynthesis in P. trichocarpa SDX; one converts p-coumaric acid to caffeic acid and the other converts p-coumaroyl shikimic acid to caffeoyl shikimic acid. Cinnamic acid 4-hydroxylation is also mediated by the same protein complexes. These results provide direct evidence for functional involvement of membrane protein complexes in monolignol biosynthesis.</AbstractText>
</Abstract>
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<ForeName>Jie</ForeName>
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Membrane protein complexes catalyze both 4- and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis.

Membrane protein complexes catalyze both 4- and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis.

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