Inhibition of acetyl phosphate-dependent transcription by an acetylatable lysine on RNA polymerase

J Biol Chem. 2012 Sep 14;287(38):32147-60. doi: 10.1074/jbc.M112.365502. Epub 2012 Jul 24.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Physiological Phenomena
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Cloning, Molecular
  • DNA-Directed RNA Polymerases / chemistry*
  • Escherichia coli / metabolism
  • Gene Expression Regulation, Enzymologic
  • Glucose / chemistry
  • Ions
  • Lysine / chemistry*
  • Membrane Proteins / genetics*
  • Models, Chemical
  • Models, Genetic
  • Mutagenesis, Site-Directed
  • Mutation
  • Phosphates / chemistry*
  • Phosphorylation
  • Promoter Regions, Genetic
  • Protein Processing, Post-Translational

Substances

  • Bacterial Proteins
  • CpxP protein, bacteria
  • Ions
  • Membrane Proteins
  • Phosphates
  • DNA-Directed RNA Polymerases
  • Glucose
  • Lysine