Crystal structure of the 14-subunit RNA polymerase I

Nature. 2013 Oct 31;502(7473):644-9. doi: 10.1038/nature12636. Epub 2013 Oct 23.


Protein biosynthesis depends on the availability of ribosomes, which in turn relies on ribosomal RNA production. In eukaryotes, this process is carried out by RNA polymerase I (Pol I), a 14-subunit enzyme, the activity of which is a major determinant of cell growth. Here we present the crystal structure of Pol I from Saccharomyces cerevisiae at 3.0 Å resolution. The Pol I structure shows a compact core with a wide DNA-binding cleft and a tightly anchored stalk. An extended loop mimics the DNA backbone in the cleft and may be involved in regulating Pol I transcription. Subunit A12.2 extends from the A190 jaw to the active site and inserts a transcription elongation factor TFIIS-like zinc ribbon into the nucleotide triphosphate entry pore, providing insight into the role of A12.2 in RNA cleavage and Pol I insensitivity to α-amanitin. The A49-A34.5 heterodimer embraces subunit A135 through extended arms, thereby contacting and potentially regulating subunit A12.2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Crystallography, X-Ray
  • DNA / chemistry
  • DNA / metabolism
  • Models, Molecular
  • Peptide Chain Elongation, Translational
  • Protein Binding
  • Protein Conformation
  • Protein Multimerization
  • Protein Subunits / chemistry*
  • RNA Polymerase I / chemistry*
  • RNA Polymerase II / chemistry
  • RNA Polymerase III / chemistry
  • Saccharomyces cerevisiae / enzymology*
  • Transcription, Genetic


  • Protein Subunits
  • DNA
  • RNA Polymerase II
  • RNA Polymerase I
  • RNA Polymerase III

Associated data

  • PDB/4C3H
  • PDB/4C3I
  • PDB/4C3J