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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