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Systems biology of lignin biosynthesis in Populus trichocarpa: heteromeric 4-coumaric acid:coenzyme A ligase protein complex formation, regulation, and numerical modeling.

Identifieur interne : 002029 ( Main/Exploration ); précédent : 002028; suivant : 002030

Systems biology of lignin biosynthesis in Populus trichocarpa: heteromeric 4-coumaric acid:coenzyme A ligase protein complex formation, regulation, and numerical modeling.

Auteurs : Hsi-Chuan Chen [République populaire de Chine] ; Jina Song ; Jack P. Wang ; Ying-Chung Lin ; Joel Ducoste ; Christopher M. Shuford ; Jie Liu ; Quanzi Li ; Rui Shi ; Angelito Nepomuceno ; Fikret Isik ; David C. Muddiman ; Cranos Williams ; Ronald R. Sederoff ; Vincent L. Chiang

Source :

RBID : pubmed:24619612

Descripteurs français

English descriptors

Abstract

As a step toward predictive modeling of flux through the pathway of monolignol biosynthesis in stem differentiating xylem of Populus trichocarpa, we discovered that the two 4-coumaric acid:CoA ligase (4CL) isoforms, 4CL3 and 4CL5, interact in vivo and in vitro to form a heterotetrameric protein complex. This conclusion is based on laser microdissection, coimmunoprecipitation, chemical cross-linking, bimolecular fluorescence complementation, and mass spectrometry. The tetramer is composed of three subunits of 4CL3 and one of 4CL5. 4CL5 appears to have a regulatory role. This protein-protein interaction affects the direction and rate of metabolic flux for monolignol biosynthesis in P. trichocarpa. A mathematical model was developed for the behavior of 4CL3 and 4CL5 individually and in mixtures that form the enzyme complex. The model incorporates effects of mixtures of multiple hydroxycinnamic acid substrates, competitive inhibition, uncompetitive inhibition, and self-inhibition, along with characteristic of the substrates, the enzyme isoforms, and the tetrameric complex. Kinetic analysis of different ratios of the enzyme isoforms shows both inhibition and activation components, which are explained by the mathematical model and provide insight into the regulation of metabolic flux for monolignol biosynthesis by protein complex formation.

DOI: 10.1105/tpc.113.119685
PubMed: 24619612
PubMed Central: PMC4001399


Affiliations:


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Le document en format XML

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<term>Coenzyme A Ligases (genetics)</term>
<term>Coenzyme A Ligases (metabolism)</term>
<term>Coumaric Acids (metabolism)</term>
<term>Immunoprecipitation (MeSH)</term>
<term>Lignin (biosynthesis)</term>
<term>Mass Spectrometry (MeSH)</term>
<term>Models, Biological (MeSH)</term>
<term>Populus (metabolism)</term>
<term>Propionates (MeSH)</term>
<term>RNA, Messenger (genetics)</term>
<term>Substrate Specificity (MeSH)</term>
<term>Systems Biology (MeSH)</term>
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<term>ARN messager (génétique)</term>
<term>Acides coumariques (métabolisme)</term>
<term>Biologie des systèmes (MeSH)</term>
<term>Coenzyme A ligases (génétique)</term>
<term>Coenzyme A ligases (métabolisme)</term>
<term>Immunoprécipitation (MeSH)</term>
<term>Lignine (biosynthèse)</term>
<term>Modèles biologiques (MeSH)</term>
<term>Populus (métabolisme)</term>
<term>Propionates (MeSH)</term>
<term>Spectrométrie de masse (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
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<term>Lignin</term>
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<term>RNA, Messenger</term>
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<term>Coenzyme A Ligases</term>
<term>Coumaric Acids</term>
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<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr">
<term>Lignine</term>
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<term>ARN messager</term>
<term>Coenzyme A ligases</term>
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<term>Populus</term>
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<term>Acides coumariques</term>
<term>Coenzyme A ligases</term>
<term>Populus</term>
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<term>Immunoprécipitation</term>
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<div type="abstract" xml:lang="en">As a step toward predictive modeling of flux through the pathway of monolignol biosynthesis in stem differentiating xylem of Populus trichocarpa, we discovered that the two 4-coumaric acid:CoA ligase (4CL) isoforms, 4CL3 and 4CL5, interact in vivo and in vitro to form a heterotetrameric protein complex. This conclusion is based on laser microdissection, coimmunoprecipitation, chemical cross-linking, bimolecular fluorescence complementation, and mass spectrometry. The tetramer is composed of three subunits of 4CL3 and one of 4CL5. 4CL5 appears to have a regulatory role. This protein-protein interaction affects the direction and rate of metabolic flux for monolignol biosynthesis in P. trichocarpa. A mathematical model was developed for the behavior of 4CL3 and 4CL5 individually and in mixtures that form the enzyme complex. The model incorporates effects of mixtures of multiple hydroxycinnamic acid substrates, competitive inhibition, uncompetitive inhibition, and self-inhibition, along with characteristic of the substrates, the enzyme isoforms, and the tetrameric complex. Kinetic analysis of different ratios of the enzyme isoforms shows both inhibition and activation components, which are explained by the mathematical model and provide insight into the regulation of metabolic flux for monolignol biosynthesis by protein complex formation. </div>
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