Inhibition of Acetyl Phosphate-dependent Transcription by an Acetylatable Lysine on RNA Polymerase

• Published in: The Journal of biological chemistry Vol. 287; no. 38; pp. 32147 - 32160
• Main Authors: Lima, Bruno P., Thanh Huyen, Tran Thi, Bäsell, Katrin, Becher, Dörte, Antelmann, Haike, Wolfe, Alan J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 14-09-2012; American Society for Biochemistry and Molecular Biology
• Subjects: Acetyl Coenzyme A; Acetyl Phosphate; Bacterial Physiological Phenomena; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Signal Transduction; Bacterial transcription; Central Metabolism; Cloning, Molecular; CpxAR; DNA-Directed RNA Polymerases - chemistry; Escherichia coli - metabolism; Gene Expression Regulation, Enzymologic; Glucose - chemistry; Ions; Lysine - chemistry; Lysine Acetylation; Membrane Proteins - genetics; Microbiology; Models, Chemical; Models, Genetic; Mutagenesis, Site-Directed; Mutation; Phos-Tag; Phosphates - chemistry; Phosphorylation; Promoter Regions, Genetic; Protein Processing, Post-Translational; RNA Polymerase; Phosphorylation; Phos-Tag; Bacterial Signal Transduction; Central Metabolism; Lysine Acetylation; CpxAR; Bacterial transcription; Acetyl Coenzyme A; RNA Polymerase; Acetyl Phosphate
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M112.365502

The ability of bacteria to adapt to environmental changes has allowed these organisms to thrive in all parts of the globe. By monitoring their extracellular and intracellular environments, bacteria assure their most appropriate response for each environment. Post-translational modification of proteins is one mechanism by which cells respond to their changing environments. Here, we report that two post-translational modifications regulate transcription of the extracytoplasmic stress-responsive promoter cpxP: (i) acetyl phosphate-dependent phosphorylation of the response regulator CpxR and (ii) acetyl coenzyme A-dependent acetylation of the α subunit of RNA polymerase. Together, these two post-translational modifications fine-tune cpxP transcription in response to changes in the intracellular environment.
Background: Phosphorylation and acetylation are ubiquitous post-translational modifications of bacterial proteins.
Results: Glucose-induced cpxP transcription requires acetyl phosphate. This activity is inhibited by lysine 291 of the RNA polymerase α subunit, which becomes acetylated under inhibitory conditions.
Conclusion: Phosphorylation and acetylation co-regulate the cpxP promoter.
Significance: Central metabolism is implicated in the regulation of the stress-responsive promoter cpxP.