Biochemical characterization of caffeoyl coenzyme A 3-O-methyltransferase from wheat
العنوان: | Biochemical characterization of caffeoyl coenzyme A 3-O-methyltransferase from wheat |
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المؤلفون: | Qing-Hu Ma, Hao-Ran Luo |
المصدر: | Planta. 242:113-122 |
بيانات النشر: | Springer Science and Business Media LLC, 2015. |
سنة النشر: | 2015 |
مصطلحات موضوعية: | Plant Science, Gene Expression Regulation, Enzymologic, Substrate Specificity, law.invention, chemistry.chemical_compound, Biosynthesis, Gene Expression Regulation, Plant, law, Genetics, Lignin, Gene, Phylogeny, Triticum, Regulation of gene expression, chemistry.chemical_classification, Plant Stems, biology, Temperature, Gene Expression Regulation, Developmental, food and beverages, Methyltransferases, Hydrogen-Ion Concentration, O-methyltransferase, Recombinant Proteins, Enzyme assay, Kinetics, Enzyme, Biochemistry, chemistry, biology.protein, Recombinant DNA |
الوصف: | TaCCoAOMT1 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. |
تدمد: | 1432-2048 0032-0935 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ed6876d6eb55b7d9969a6d222b652ec https://doi.org/10.1007/s00425-015-2295-3 |
حقوق: | CLOSED |
رقم الأكسشن: | edsair.doi.dedup.....5ed6876d6eb55b7d9969a6d222b652ec |
قاعدة البيانات: | OpenAIRE |
تدمد: | 14322048 00320935 |
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