title: The roles of bacterial GCN5-related N-acetyltransferases.
abstract: The GCN5-related N-acetyltransferase (GNAT) superfamily of proteins, widespread in eukaryotes and prokaryotes, can utilize acyl coenzyme A (acyl CoA) to acylate respective acceptor substrates and release both CoA and the acylated products. GNATs have been shown to be involved in multiple physiological events, including bacterial drug resistance, regulation of transcription, stress reaction, and metabolic flux, etc. In the last few years, the importance of GNATs has only emerged in eukaryotes, but bacterial GNATs, particularly those of pathogens, have only recently been explored. In this review, we summarize the main members, structures, inhibitors, and activators of proteins in the GNAT family. We focus on the roles of GNATs in bacteria, particularly Mycobacterium tuberculosis GNATs.
authors.affiliation: Institute of Modern Biopharmaceuticals, state Key Laboratory Breeding Base of Ministry of Education Eco-Environment of the Three Gorges Reservoir Region, School of Life Sciences, Southwest University, Beibei, Chongqing, China.
authors.forename: Longxiang
authors.initials: L
authors.lastname: Xie
authors.affiliation: Institute of Modern Biopharmaceuticals, State Key Laboratory Breeding Base of Eco-Environment and Bio-Resource of the Three Gorges Area, School of Life Sciences, Southwest University, Beibei, Chongqing, China.
authors.forename: Jie
authors.initials: J
authors.lastname: Zeng
authors.affiliation: Institute of Modern Biopharmaceuticals, state Key Laboratory Breeding Base of Ministry of Education Eco-Environment of the Three Gorges Reservoir Region, School of Life Sciences, Southwest University, Beibei, Chongqing, China.
authors.forename: Hongping
authors.initials: H
authors.lastname: Luo
authors.affiliation: Department of Microbiology and Molecular Genetics, Department of Dermatology, Changzheng Hospital, Institute of Medical Mycology, Shanghai Key Laboratory of Molecular Medical Mycology, Second Military Medical University, Shanghai, P.R. China.
authors.forename: Weihua
authors.initials: W
authors.lastname: Pan
authors.affiliation: Institute of Modern Biopharmaceuticals, State Key Laboratory Breeding Base of Eco-Enviroment and Bio-Resource of the Three Gorges Area, School of Life Sciences, Southwest University, Beibei, Chongqing, China.
authors.forename: Jianping
authors.initials: J
authors.lastname: Xie
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D019295:Computational Biology; D024881:Drug Resistance, Bacterial / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial; D051548:Histone Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D009169:Mycobacterium tuberculosis / Q000201:enzymology* / Q000235:genetics*
chemical_list: D001426:Bacterial Proteins; D051548:Histone Acetyltransferases