- PDB-2rf4: Crystal structure of the RNA Polymerase I subcomplex A14/43 -
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Basic information
Entry
Database: PDB / ID: 2rf4
Title
Crystal structure of the RNA Polymerase I subcomplex A14/43
Components
(DNA-directed RNA polymerase I subunit RPA4) x 2
Keywords
TRANSFERASE / Transferase DNA/RNA / DNA-binding / Phosphorylation / RNA Polymerase I / Pol I / PolI / RPolI / Nuclear Protein / Nucleolar Protein / Transcription / DDRP / Rpb4/7 / Ribosome biogenesis / DNA-directed RNA polymerase / Nucleus
Function / homology
Function and homology information
RNA Polymerase I Transcription Initiation / regulation of cell size / termination of RNA polymerase I transcription / RNA Polymerase I Promoter Escape / nucleolar large rRNA transcription by RNA polymerase I / transcription initiation at RNA polymerase I promoter / transcription by RNA polymerase I / transcription elongation by RNA polymerase I / RNA polymerase I activity / RNA polymerase I complex ...RNA Polymerase I Transcription Initiation / regulation of cell size / termination of RNA polymerase I transcription / RNA Polymerase I Promoter Escape / nucleolar large rRNA transcription by RNA polymerase I / transcription initiation at RNA polymerase I promoter / transcription by RNA polymerase I / transcription elongation by RNA polymerase I / RNA polymerase I activity / RNA polymerase I complex / ribosome biogenesis / nucleus Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #3390 / RNA polymerase I, subunit Rpa14, fungi / Yeast RNA polymerase I subunit RPA14 / Rpa43, N-terminal ribonucleoprotein (RNP) domain / RNA polymerase Rpb7-like, N-terminal domain / RPA43, OB domain / RPA43 OB domain in RNA Pol I / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / RNA polymerase subunit Rpb7-like / RNA polymerase Rpb7-like , N-terminal ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #3390 / RNA polymerase I, subunit Rpa14, fungi / Yeast RNA polymerase I subunit RPA14 / Rpa43, N-terminal ribonucleoprotein (RNP) domain / RNA polymerase Rpb7-like, N-terminal domain / RPA43, OB domain / RPA43 OB domain in RNA Pol I / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / RNA polymerase subunit Rpb7-like / RNA polymerase Rpb7-like , N-terminal / RNA polymerase Rpb7-like, N-terminal domain superfamily / SHS2 domain found in N terminus of Rpb7p/Rpc25p/MJ0397 / Nucleic acid-binding proteins / Dna Ligase; domain 1 / Helix non-globular / Special / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Nucleic acid-binding, OB-fold / Beta Barrel / 2-Layer Sandwich / Mainly Beta / Alpha Beta Similarity search - Domain/homology
DNA-directed RNA polymerase I subunit RPA43 / DNA-directed RNA polymerase I subunit RPA14 Similarity search - Component
Biological species
Saccharomyces cerevisiae (brewer's yeast)
Method
X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.1 Å
Journal: Cell / Year: 2007 Title: Functional architecture of RNA polymerase I. Authors: Claus-D Kuhn / Sebastian R Geiger / Sonja Baumli / Marco Gartmann / Jochen Gerber / Stefan Jennebach / Thorsten Mielke / Herbert Tschochner / Roland Beckmann / Patrick Cramer / 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 ...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.
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