Kuhn, Claus-D. and Geiger, Sebastian R. and Baumli, Sonja and Gartmann, Marco and Gerber, Jochen and Jennebach, Stefan and Mielke, Thorsten and Tschochner, Herbert and Beckmann, Roland and Cramer, Patrick (2007) Functional architecture of RNA polymerase I. CELL, 131 (7). pp. 1260-1272. ISSN 0092-8674, 1097-4172
Full text not available from this repository. (Request a copy)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 angstrom cryoelectron 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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | INTRINSIC TRANSCRIPT CLEAVAGE; SACCHAROMYCES-CEREVISIAE; ELECTRON-MICROSCOPY; PREINITIATION COMPLEX; ELONGATION COMPLEX; III SUBUNITS; H ACTIVITY; YEAST; INITIATION; TERMINATION; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie III > Prof. Dr. Herbert Tschochner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 25 Nov 2020 06:26 |
| Last Modified: | 25 Nov 2020 06:26 |
| URI: | https://pred.uni-regensburg.de/id/eprint/31796 |
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