title: Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase.
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.
authors: Key Laboratory of Agricultural and Environmental Microbiology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China.
authors: Qun-Fang
authors: QF
authors: Zhang
authors: Qunfang
authors: Q
authors: Zhang
authors: Jing
authors: J
authors: Gu
authors: Peng
authors: P
authors: Gong
authors: Xu-De
authors: XD
authors: Wang
authors: Xude
authors: X
authors: Wang
authors: Shun
authors: S
authors: Tu
authors: Li-Jun
authors: LJ
authors: Bi
authors: Lijun
authors: L
authors: Bi
authors: Zi-Niu
authors: ZN
authors: Yu
authors: Ziniu
authors: Z
authors: Yu
authors: Zhi-Ping
authors: ZP
authors: Zhang
authors: Zhiping
authors: Z
authors: Zhang
authors: Zong-Qiang
authors: ZQ
authors: Cui
authors: Zongqiang
authors: Z
authors: Cui
authors: Hong-Ping
authors: HP
authors: Wei
authors: Hongping
authors: H
authors: Wei
authors: Sheng-Ce
authors: SC
authors: Tao
authors: Shengce
authors: S
authors: Tao
authors: Xian En
authors: XE
authors: Zhang
authors: Xianen
authors: X
authors: Zhang
authors: Jiao-Yu
authors: JY
authors: Deng
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008239:Lysine / Q000031:analogs & derivatives; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010446:Peptide Fragments / Q000737:chemistry; D040081:Protein Array Analysis; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000378:metabolism; D037761:Sirtuins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D029968:Escherichia coli Proteins; D010446:Peptide Fragments; D020543:Proteome; C002315:N(alpha)-acetyllysine; D000123:Acetyltransferases; C019736:N-hydroxyarylamine O-acetyltransferase; D037761:Sirtuins; C483998:cobB protein, E Coli; D008239:Lysine