title: Lysine acetylation regulates the activity of Escherichia coli S-adenosylmethionine synthase.
abstract: Lysine acetylation is one of the most abundant post-translational modifications. However, physiological roles of this modification in bacteria are largely unknown. Previous protein acetylome analysis showed that Escherichia coli adenosylmethionine synthase (MAT) undergoes acetylation in vivo, but the biological functions of this modification still need to be uncovered. In this study, MAT of E. coli was over-expressed and purified. Subsequent mass spectrometry analysis showed that 12 lysine residues of the protein were acetylated. Site-directed mutagenesis analysis was performed and the results showed that acetylated lysine residues play important roles in the enzymatic activity of MAT. Next, deacetylation assay was performed by using CobB as the deacetylase, and the results showed that CobB could deacetylate MAT in vitro In addition, the enzymatic activities of acetylated and deacetylated MAT were compared in vitro, and results showed that acetylation led to a decrease in its enzymatic activity, which could be reversed by CobB deacetylation. Altogether, our data suggest that CobB modulates the enzymatic activity of E. coli MAT in vitro.
authors.affiliation: Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China University of Chinese Academy of Sciences, Beijing 100039, China.
authors.forename: Manluan
authors.initials: M
authors.lastname: Sun
authors.affiliation: State Key Lab of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.
authors.forename: Hongsen
authors.initials: H
authors.lastname: Guo
authors.affiliation: Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China University of Chinese Academy of Sciences, Beijing 100039, China.
authors.forename: Guoliang
authors.initials: G
authors.lastname: Lu
authors.affiliation: Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
authors.forename: Jing
authors.initials: J
authors.lastname: Gu
authors.affiliation: Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
authors.forename: Xude
authors.initials: X
authors.lastname: Wang
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China zhangxe@sun5.ibp.ac.cn dengjy@wh.iov.cn.
authors.forename: Xian-En
authors.initials: XE
authors.lastname: Zhang
authors.affiliation: Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China zhangxe@sun5.ibp.ac.cn dengjy@wh.iov.cn.
authors.forename: Jiaoyu
authors.initials: J
authors.lastname: Deng
mesh_terms: D000107:Acetylation; D004926:Escherichia coli / Q000201:enzymology*; D008239:Lysine / Q000378:metabolism*; D008716:Methionine Adenosyltransferase / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D008716:Methionine Adenosyltransferase; D008239:Lysine
keywords: CobB; S-adenosylmethionine synthase; deacetylation; lysine acetylation