Reversibly acetylated lysine residues play important roles in the enzymatic activity ofEscherichia coli N-hydroxyarylamineO-acetyltransferase

Autor:	Qun-Fang, Zhang, Qunfang, Zhang, Jing, Gu, Peng, Gong, Xu-De, Wang, Xude, Wang, Shun, Tu, Li-Jun, Bi, Lijun, Bi, Zi-Niu, Yu, Ziniu, Yu, Zhi-Ping, Zhang, Zhiping, Zhang, Zong-Qiang, Cui, Zongqiang, Cui, Hong-Ping, Wei, Hongping, Wei, Sheng-Ce, Tao, Shengce, Tao, Xian En, Zhang, Xianen, Zhang, Jiao-Yu, Deng
Rok vydání:	2013
Předmět:	Proteome Molecular Sequence Data Lysine Protein Array Analysis Biology medicine.disease_cause Biochemistry Acetyltransferases Escherichia coli medicine Sirtuins Amino Acid Sequence Molecular Biology chemistry.chemical_classification Escherichia coli Proteins Mutagenesis Acetylation Cell Biology Molecular biology Peptide Fragments Kinetics Enzyme Amino Acid Substitution chemistry Mutagenesis Site-Directed bacteria Protein deacetylase NAD+ kinase Protein Processing Post-Translational
Zdroj:	FEBS Journal. 280:1966-1979
ISSN:	1742-464X
DOI:	10.1111/febs.12216
Popis:	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.
Databáze:	OpenAIRE
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