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

Biochem Biophys Res Commun

State Key Laboratory of Genetic Engineering, Institute of Plant Biology, School of Life Sciences, Fudan University, Shanghai, 200438, China. Electronic address:

Published: November 2019

AI Article Synopsis

  • Dietary phenolic compounds, such as anthocyanins and flavonoids, exhibit strong antioxidant and health benefits, with ferulate being a key compound derived from caffeoyl CoA.* -
  • The study identifies Arabidopsis CCoAOMT7, which plays a significant role in increasing ferulate levels in the stem cell wall through its interactions with essential proteins in the SAM synthesis cycle.* -
  • Disruption of certain proteins, like SAHH1 and SAM synthases, led to a significant decrease in ferulate content, highlighting important connections between protein complexes and cellular methylation processes.*

Article 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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http://dx.doi.org/10.1016/j.bbrc.2019.09.101DOI Listing

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