Format

Send to

Choose Destination
See comment in PubMed Commons below
FEBS J. 2013 May;280(9):1966-79. doi: 10.1111/febs.12216. Epub 2013 Mar 21.

Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase.

Author information

1
Key Laboratory of Agricultural and Environmental Microbiology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China.

Erratum in

  • FEBS J. 2013 Jul;280(14):3480. Zhang, Qunfang [corrected to Zhang, Qun-Fang]; Wang, Xude [corrected to Wang, Xu-De]; Bi, Lijun [corrected to Bi, Li-Jun]; Yu, Ziniu [corrected to Yu, Zi-Niu]; Zhang, Zhiping [corrected to Zhang, Zhi-Ping]; Cui, Zongqiang [corrected to Cui, Zong-Qiang]; Wei, Hongping [corrected to Wei, Hong-Ping]; Tao, Shengce [corrected to Tao, Sheng-Ce]; Zhang, Xianen [corrected to Zhang, Xian-Xian-En]; Deng, Jiao-Yu [added].

Abstract

CobB 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 CobB were screened and nine proteins were identified, including N-hydroxyarylamine O-acetyltransferase (NhoA). In vitro acetylation/deacetylation of NhoA 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 NhoA 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 NhoA. These results suggest that reversible acetylation may play a role in the activity of Escherichia coli NhoA.

PMID:
23452042
DOI:
10.1111/febs.12216
[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley
    Loading ...
    Support Center