Functional architecture of RNA polymerase I

被引：163

作者：

Kuhn, Claus-D. ^{[1
,2
]}

Geiger, Sebastian R. ^{[1
,2
]}

Baumli, Sonja ^{[1
,2
]}

Gartmann, Marco ^{[1
,2
]}

Gerber, Jochen ^{[3
]}

Jennebach, Stefan ^{[1
,2
]}

Mielke, Thorsten ^{[4
]}

Tschochner, Herbert ^{[3
]}

Beckmann, Roland ^{[1
,2
]}

Cramer, Patrick ^{[1
,2
]}

机构：

[1] Univ Munich, Dept Chem & Biochem, Gene Ctr Munich, D-81377 Munich, Germany

[2] Univ Munich, Dept Chem & Biochem, Ctr Integrated Prot Sci CIPSM, D-81377 Munich, Germany

[3] Univ Regensburg, Inst Biochem Genet & Mikrobiol, D-93053 Regensburg, Germany

[4] Max Planck Inst Mol Genet, D-14195 Berlin, Germany

来源：

CELL | 2007年 / 131卷 / 07期

关键词：

D O I：

10.1016/j.cell.2007.10.051

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1260 / 1272

页数：13

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