Crystal structure of the 14-subunit RNA polymerase I

Research output: Contribution to journalJournal articleResearchpeer-review

  • Carlos Fernández-Tornero
  • María Moreno-Morcillo
  • Umar J Rashid
  • Taylor, Nicholas M I
  • Federico M Ruiz
  • Tim Gruene
  • Pierre Legrand
  • Ulrich Steuerwald
  • Christoph W Müller

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.

Original languageEnglish
Issue number7473
Pages (from-to)644-9
Number of pages6
Publication statusPublished - 2013
Externally publishedYes

    Research areas

  • Catalytic Domain, Crystallography, X-Ray, DNA/chemistry, 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

ID: 194520972