Structural biology of bacterial RNA polymerase

Biomolecules. 2015 May 11;5(2):848-64. doi: 10.3390/biom5020848.

Abstract

Since its discovery and characterization in the early 1960s (Hurwitz, J. The discovery of RNA polymerase. J. Biol. Chem. 2005, 280, 42477-42485), an enormous amount of biochemical, biophysical and genetic data has been collected on bacterial RNA polymerase (RNAP). In the late 1990s, structural information pertaining to bacterial RNAP has emerged that provided unprecedented insights into the function and mechanism of RNA transcription. In this review, I list all structures related to bacterial RNAP (as determined by X-ray crystallography and NMR methods available from the Protein Data Bank), describe their contributions to bacterial transcription research and discuss the role that small molecules play in inhibiting bacterial RNA transcription.

Keywords: NMR; X-ray crystallography; anti-σ factor; bacterial RNA polymerase; core enzyme; holoenzyme; inhibitor antibiotic; transcription; transcription factor; σ factor.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / antagonists & inhibitors
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • DNA-Directed RNA Polymerases / antagonists & inhibitors
  • DNA-Directed RNA Polymerases / chemistry*
  • DNA-Directed RNA Polymerases / metabolism
  • Enzyme Inhibitors / pharmacology
  • Molecular Sequence Data

Substances

  • Bacterial Proteins
  • Enzyme Inhibitors
  • DNA-Directed RNA Polymerases