Functional architecture of RNA polymerase I

Claus-D Kuhn; Sebastian R Geiger; Sonja Baumli; Marco Gartmann; Jochen Gerber; Stefan Jennebach; Thorsten Mielke; Herbert Tschochner; Roland Beckmann; Patrick Cramer

doi:10.1016/j.cell.2007.10.051

Functional architecture of RNA polymerase I

Cell. 2007 Dec 28;131(7):1260-72. doi: 10.1016/j.cell.2007.10.051.

Authors

Claus-D Kuhn¹, Sebastian R Geiger, Sonja Baumli, Marco Gartmann, Jochen Gerber, Stefan Jennebach, Thorsten Mielke, Herbert Tschochner, Roland Beckmann, Patrick Cramer

Affiliation

¹ Gene Center Munich and Center for Integrated Protein Science CIPSM, Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universität München, Feodor-Lynen-Str. 25, 81377 Munich, Germany.

PMID: 18160037
DOI: 10.1016/j.cell.2007.10.051

Abstract

Synthesis of ribosomal RNA (rRNA) by RNA polymerase (Pol) I is the first step in ribosome biogenesis and a regulatory switch in eukaryotic cell growth. Here we report the 12 A cryo-electron microscopic structure for the complete 14-subunit yeast Pol I, a homology model for the core enzyme, and the crystal structure of the subcomplex A14/43. In the resulting hybrid structure of Pol I, A14/43, the clamp, and the dock domain contribute to a unique surface interacting with promoter-specific initiation factors. The Pol I-specific subunits A49 and A34.5 form a heterodimer near the enzyme funnel that acts as a built-in elongation factor and is related to the Pol II-associated factor TFIIF. In contrast to Pol II, Pol I has a strong intrinsic 3'-RNA cleavage activity, which requires the C-terminal domain of subunit A12.2 and, apparently, enables ribosomal RNA proofreading and 3'-end trimming.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Binding Sites
Cryoelectron Microscopy
Crystallography, X-Ray
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 Interaction Mapping
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