IB-CAS  > 中科院北方资源植物重点实验室
Biochemical characterization of caffeoyl coenzyme A 3-O-methyltransferase from wheat
Ma, Qing-Hu; Luo, Hao-Ran
2015
Source PublicationPLANTA
ISSN0032-0935
Volume242Issue:1Pages:113-122
AbstractTaCCoAOMT1 is located in wheat chromosome 7A and highly expressed in stem and root. It is important for lignin biosynthesis, and associated with stem maturity but not lodging resistance. Caffeoyl coenzyme A 3-O-methyltransferases (CCoAOMTs) are one important class of enzymes to carry out the transfer of the methyl group from S-adenosylmethionine to the hydroxyl group, and play important roles in lignin and flavonoids biosynthesis. In the present study, sequences for CCoAOMT from the wheat genome were analyzed. One wheat CCoAOMT that belonged to bona fide subclade involved in lignin biosynthesis, namely TaCCoAOMT1, was obtained by the prokaryotic expression in E. coli. The three-dimensional structure prediction showed a highly similar structure of TaCCoAOMT1 with MsCCoAOMT. Recombinant TaCCoAOMT1 protein could only use caffeoyl CoA and 5-hydroxyferuloyl CoA as effective substrates and caffeoyl CoA as the best substrate. TaCCoAOMT1 had a narrow optimal pH and thermal stability. The TaCCoAOMT1 gene was highly expressed in wheat stem and root tissues, paralleled CCoAOMT enzyme activity. TaCCoAOMT1 mRNA abundance and enzyme activity increased linearly with stem maturity, but showed little difference between wheat lodging-resistant (H4546) and lodging-sensitive (C6001) cultivars in elongation, heading and milky stages. These data suggest that TaCCoAOMT1 is an important CCoAOMT for lignin biosynthesis that is critical for stem development, but not directly associated with lodging-resistant trait in wheat.
KeywordCaffeoyl coenzyme A 3-O-methyltransferase (CCoAOMT) Lignin biosynthesis Lodging resistance Stem development Triticum
Subject AreaPlant Sciences
DOI10.1007/s00425-015-2295-3
Indexed BySCI
Language英语
WOS KeywordCELL-SUSPENSION CULTURES ; ADENOSYL-L-METHIONINE ; ACID/5-HYDROXYFERULIC ACID 3/5-O-METHYLTRANSFERASE ; CINNAMOYL-COA REDUCTASE ; O-METHYLTRANSFERASE ; LIGNIN BIOSYNTHESIS ; ARABIDOPSIS-THALIANA ; DOWN-REGULATION ; METHYLATION PATHWAY ; PHENYLPROPANOID METABOLISM
WOS Research AreaScience Citation Index Expanded (SCI-EXPANDED)
WOS IDWOS:000356516800008
PublisherSPRINGER
SubtypeArticle
Publication PlaceNEW YORK
EISSN1432-2048
Funding OrganizationNational Natural Science Foundation of China [31370336, 31170277] ; National Key Basic Research Program of China (973 program) ; Natural Science Foundation of Beijing [5122024] ; Innovation Project of Chinese Academy of Sciences
Corresponding Author Emailmqh@ibcas.ac.cn
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Document Type期刊论文
Identifierhttp://ir.ibcas.ac.cn/handle/2S10CLM1/25585
Collection中科院北方资源植物重点实验室
Affiliation1.[Ma, Qing-Hu
2.Chinese Acad Sci, Inst Bot, Key Lab Plant Resources, Beijing 100093, Peoples R China
3.Chinese Acad Sci, Inst Bot, Beijing Bot Garden, Beijing 100093, Peoples R China
Recommended Citation
GB/T 7714
Ma, Qing-Hu,Luo, Hao-Ran. Biochemical characterization of caffeoyl coenzyme A 3-O-methyltransferase from wheat[J]. PLANTA,2015,242(1):113-122.
APA Ma, Qing-Hu,&Luo, Hao-Ran.(2015).Biochemical characterization of caffeoyl coenzyme A 3-O-methyltransferase from wheat.PLANTA,242(1),113-122.
MLA Ma, Qing-Hu,et al."Biochemical characterization of caffeoyl coenzyme A 3-O-methyltransferase from wheat".PLANTA 242.1(2015):113-122.
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