Document Detail


Membrane protein complexes catalyze both 4- and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis.
MedLine Citation:
PMID:  22160716     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Hsi-Chuan Chen; Quanzi Li; Christopher M Shuford; Jie Liu; David C Muddiman; Ronald R Sederoff; Vincent L Chiang
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2011-12-12
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  108     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2011 Dec 
Date Detail:
Created Date:  2011-12-28     Completed Date:  2012-02-21     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  21253-8     Citation Subset:  IM    
Affiliation:
Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695, USA.
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MeSH Terms
Descriptor/Qualifier:
Carboxylic Ester Hydrolases / chemistry,  metabolism*
Chromatography, Liquid
DNA Primers / genetics
Hydroxylation
Immunoprecipitation
Kinetics
Lignin / biosynthesis*
Mass Spectrometry
Membrane Proteins / chemistry,  metabolism*
Microscopy, Confocal
Molecular Structure
Multiprotein Complexes / chemistry,  metabolism*
Phenols
Phenylpropionates
Plasmids / genetics
Populus / metabolism*
Propionates
Trans-Cinnamate 4-Monooxygenase / chemistry,  metabolism*
Xylem / metabolism*
Yeasts
Chemical
Reg. No./Substance:
0/DNA Primers; 0/Membrane Proteins; 0/Multiprotein Complexes; 0/Phenols; 0/Phenylpropionates; 0/Propionates; 0/sinapyl alcohol; 0/trans-3-(4'-hydroxyphenyl)-2-propenoic acid; 9005-53-2/Lignin; E7SM92591P/coniferyl alcohol; EC 1.14.13.11/Trans-Cinnamate 4-Monooxygenase; EC 3.1.1.-/Carboxylic Ester Hydrolases; EC 3.1.1.-/trans-4-coumaroyl esterase
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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