title: Bacterial protein acetylation: new discoveries unanswered questions.
abstract: Nε-acetylation is emerging as an abundant post-translational modification of bacterial proteins. Two mechanisms have been identified: one is enzymatic, dependent on an acetyltransferase and acetyl-coenzyme A; the other is non-enzymatic and depends on the reactivity of acetyl phosphate. Some, but not most, of those acetylations are reversed by deacetylases. This review will briefly describe the current status of the field and raise questions that need answering.
authors.affiliation: Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, 2160 S. First Ave., Bldg. 105, Maywood, IL, 60153, USA. awolfe@luc.edu.
authors.forename: Alan J
authors.initials: AJ
authors.lastname: Wolfe
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D006801:Humans; D010755:Organophosphates / Q000378:metabolism; D011499:Protein Processing, Post-Translational
chemical_list: D001426:Bacterial Proteins; D010755:Organophosphates; C011632:acetyl phosphate; D000123:Acetyltransferases
keywords: Acetyl phosphate; Acetyltransferase; CRP; Deacetylase; Metabolism; Post-translational modification