Structure of an archaeal RNA polymerase

J Mol Biol. 2008 Feb 15;376(2):303-7. doi: 10.1016/j.jmb.2007.08.066. Epub 2007 Sep 5.

Abstract

Related multisubunit RNA polymerases (RNAPs) carry out gene transcription in all kingdoms of life. Since structural information is limited to bacterial and eukaryotic RNAPs, we determined the cryo-electron microscopic structure of the RNAP from the thermophilic archaeon Pyrococcus furiosus at 13 A resolution. Comparison with eukaryotic RNAP II reveals a conserved architecture, no homologues for subunits Rpb8 and Rpb9, and significant deviation in the polymerase foot, jaws, pore, and protrusion. The structural organization of the archaeal RNA polymerase serves as a reference for future structure-function analysis of the transcription mechanism and allows for evolutionary comparisons.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Archaeal Proteins / chemistry
  • Binding Sites
  • DNA / metabolism
  • DNA-Directed RNA Polymerases / chemistry*
  • DNA-Directed RNA Polymerases / isolation & purification
  • DNA-Directed RNA Polymerases / physiology
  • DNA-Directed RNA Polymerases / ultrastructure
  • Eukaryotic Cells
  • Models, Molecular
  • Protein Conformation
  • Protein Structure, Tertiary
  • Protein Subunits / chemistry
  • Pyrococcus furiosus / enzymology
  • Pyrococcus furiosus / genetics
  • RNA / biosynthesis
  • Structure-Activity Relationship
  • Transcription, Genetic

Substances

  • Archaeal Proteins
  • Protein Subunits
  • RNA
  • DNA
  • DNA-Directed RNA Polymerases