title: Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter.
abstract: In eukaryotes, lysine acetylation is a well-established post-translational modification that has been implicated in virtually all aspects of eukaryotic physiology. Although homologues of the enzymes that catalyse protein acetylation are widely conserved and distributed among bacterial species, not much is known about the impact of protein acetylation on bacterial physiology. Here, we present evidence that the Gcn5-like acetyltransferase YfiQ and the sirtuin deacetylase CobB play crucial roles in the transcription regulation of the periplasmic stress-responsive promoter cpxP when cells of Escherichia coli grow in the presence of glucose, an environment that induces protein acetylation. Under this growth condition, several acetylation sites were detected on three of the RNA polymerase subunits: β, β' and α. We focused on acetylations of the carboxy-terminal domain (CTD) of α because of its relative small size and its limited acetylation. We determined that K298 of α is acetylated in a glucose and YfiQ-dependent manner and that K298 is specifically required for glucose-induced cpxP transcription. Because the αCTD aids in promoter recognition by RNA polymerase, we propose its acetylation may influence bacterial physiology through effects on gene expression.
authors.affiliation: Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, Maywood, IL 60153, USA.
authors.forename: Bruno P
authors.initials: BP
authors.lastname: Lima
authors.forename: Haike
authors.initials: H
authors.lastname: Antelmann
authors.forename: Katrin
authors.initials: K
authors.lastname: Gronau
authors.forename: Bui Khanh
authors.initials: BK
authors.lastname: Chi
authors.forename: Dörte
authors.initials: D
authors.lastname: Becher
authors.forename: Shaun R
authors.initials: SR
authors.lastname: Brinsmade
authors.forename: Alan J
authors.initials: AJ
authors.lastname: Wolfe
mesh_terms: D000105:Acetyl Coenzyme A / Q000378:metabolism; D000107:Acetylation; D000123:Acetyltransferases / Q000235:genetics* / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000096:biosynthesis* / Q000235:genetics* / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D005947:Glucose / Q000378:metabolism*; D008239:Lysine / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000096:biosynthesis*; D011401:Promoter Regions, Genetic; D011499:Protein Processing, Post-Translational; D037761:Sirtuins / Q000235:genetics* / Q000378:metabolism; D013312:Stress, Physiological / Q000235:genetics*; D014158:Transcription, Genetic
chemical_list: C491730:CpxP protein, E coli; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000105:Acetyl Coenzyme A; D000123:Acetyltransferases; C561243:acetyl-CoA synthetase acetylase, E coli; D012321:DNA-Directed RNA Polymerases; C113275:RNA polymerase alpha subunit; D037761:Sirtuins; C483998:cobB protein, E Coli; D005947:Glucose; D008239:Lysine