分子生物学
IVD分子诊断
细胞培养与分析
蛋白研究
细胞因子
重组蛋白
抗体
高通量测序建库
病原检测UCF系列
生物医药
工具酶
抑制剂激活剂与常用试剂
仪器
耗材

SAHH and SAMS form a methyl donor complex with CCoAOMT7 for methylation of phenolic compounds

Shu-Xian Yang, Tian-Tian Wu, Ci-Hang Ding, Peng-Cheng Zhou, Zhong-Zhong Chen, Jin-Ying Gou

Journal:BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

IF:2.71

DOI:10.1016/j.bbrc.2019.09.101

PMID:31582217

Published:2019-09-30

research field:分子生物学植物生物化学代谢学

Abstract

A wealth of studies illustrate the powerful antioxidant activities and health-promoting functions of dietary phenolic compounds, e.g., anthocyanins , flavonoids , and phenolic compounds. Ferulate is methylated from caffeoyl CoA using S-adenosyl-L-methionine (SAM) as methyl donor catalyzed by caffeoyl CoA methyltransferase (CCoAOMT). Here we show that Arabidopsis CCoAOMT7 contributes to ferulate content in the stem cell wall. CCoAOMT7 was further shown to bind S-adenosyl-L-homocysteine hydrolase (SAHH), a critical step in SAM synthesis to release feedback suppression on CCoAOMT. CCoAOMT7 also bound S-adenosyl-L-methionine synthases (SAMSs) in vivo , which were mediated by SAHH1. Interruptions of endogenous SAHH1 by artificial miRNA or SAMSs by T-DNA insertion significantly reduced ferulate contents in the stem cell wall. This data reveals a novel protein complex of SAM synthesis cycle associated with O-methyltransferase and provides new insights into cellular methylation processes.

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