RNA polymerase I: a multifunctional molecular machine

Cell. 2007 Dec 28;131(7):1224-5. doi: 10.1016/j.cell.2007.12.005.

Abstract

In this issue, Kuhn et al. (2007) report the complete structure of the 14-subunit yeast RNA polymerase (Pol) I enzyme at 12 A resolution using cryo-electron microscopy (cryo-EM). Their study reveals that three subunits of Pol I perform functions in transcription elongation that are outsourced to the transcription factors TFIIF and TFIIS in the analogous Pol II transcription system.

Publication types

  • Comment

MeSH terms

  • Binding Sites
  • DNA Polymerase I / chemistry*
  • DNA Polymerase I / genetics
  • DNA Polymerase I / metabolism
  • Models, Molecular
  • Mutation
  • Peptide Elongation Factors / chemistry
  • Peptide Elongation Factors / metabolism
  • Peptide Initiation Factors / chemistry
  • Peptide Initiation Factors / metabolism
  • Promoter Regions, Genetic
  • Protein Conformation
  • Protein Interaction Domains and Motifs
  • Protein Structure, Tertiary
  • Protein Subunits
  • RNA Processing, Post-Transcriptional*
  • RNA, Ribosomal / genetics
  • RNA, Ribosomal / metabolism*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Structure-Activity Relationship
  • Transcription Factors, TFII / chemistry
  • Transcription Factors, TFII / metabolism
  • Transcription, Genetic*
  • Transcriptional Elongation Factors / chemistry
  • Transcriptional Elongation Factors / metabolism

Substances

  • Peptide Elongation Factors
  • Peptide Initiation Factors
  • Protein Subunits
  • RNA, Ribosomal
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors, TFII
  • Transcriptional Elongation Factors
  • transcription factor S-II
  • DNA Polymerase I
  • POL1 protein, S cerevisiae
  • transcription factor TFIIF