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Kuhn CD, et al.  (2007) Functional architecture of RNA polymerase I. Cell 131(7):1260-72

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.

Status: Published Type: Journal Article PubMed ID: 18160037

Topics addressed in this paper

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Topics Genes linked to topics (#1 - 10 )
RPA12 RPA135 RPA14 RPA190 RPA34 RPA43 RPA49 RPB10 RPB5 RPB8
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Topics Genes linked to topics (#11 - 14 )
RPC10 RPC19 RPC40 RPO26
Function/Process blue ball blue ball blue ball blue ball
Fungal Related Genes/Proteins blue ball blue ball
Primary Literature blue ball blue ball blue ball blue ball
Protein-protein Interactions blue ball blue ball blue ball blue ball
Protein/Nucleic Acid Structure blue ball blue ball blue ball blue ball

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