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-Structure paper
Title | Functional architecture of RNA polymerase I. |
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Journal, issue, pages | Cell, Vol. 131, Issue 7, Page 1260-1272, Year 2007 |
Publish date | Dec 28, 2007 |
Authors | Claus-D Kuhn / Sebastian R Geiger / Sonja Baumli / Marco Gartmann / Jochen Gerber / Stefan Jennebach / Thorsten Mielke / Herbert Tschochner / Roland Beckmann / Patrick Cramer / |
PubMed 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. |
External links | Cell / PubMed:18160037 |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.1 - 11.9 Å |
Structure data | EMDB-1435: PDB-2rf4: |
Source |
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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 |