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Reversibly acetylated lysine residues play important roles in the enzymatic activity of E scherichia coli N ‐hydroxyarylamine O ‐acetyltransferase
Author(s) -
Zhang Qunfang,
Gu Jing,
Gong Peng,
Wang Xude,
Tu Shun,
Bi Lijun,
Yu Ziniu,
Zhang Zhiping,
Cui Zongqiang,
Wei Hongping,
Tao Shengce,
Zhang Xianen
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12216
Subject(s) - acetylation , acetyltransferase , lysine , escherichia coli , biochemistry , proteome , chemistry , enzyme , biology , microbiology and biotechnology , amino acid , gene
Cob B is a bacterial NAD + ‐dependent protein deacetylase. Although progress has been made in functional studies of this protein in recent years, its substrates and biological functions are still largely unclear. Using proteome microarray technology, potential substrates of Escherichia coli C ob B were screened and nine proteins were identified, including N ‐hydroxyarylamine O ‐acetyltransferase ( N ho A ). In vitro acetylation/deacetylation of N ho A was verified by western blotting and mass spectrometry, and two acetylated lysine residues were identified. Site‐specific mutagenesis experiments showed that mutation of each acetylated lysine decreased the acetylation level of NhoA in vitro . Further analysis showed that variant N ho A proteins carrying substitutions at the two acetylated lysine residues are involved in both the O ‐acetyltransferase and N ‐acetyltransferase activity of NhoA. Structural analyses were also performed to explore the effects of the acetylated lysine residues on the activity of N ho A . These results suggest that reversible acetylation may play a role in the activity of E scherichia coli N ho A .