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RNA polymerase I–Rrn3 complex at 4.8 Å resolution
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Journal Article
RNA polymerase I–Rrn3 complex at 4.8 Å resolution
2016
Overview
Transcription of ribosomal DNA by RNA polymerase I (Pol I) requires the initiation factor Rrn3. Here we report the cryo-EM structure of the Pol I–Rrn3 complex at 4.8 Å resolution. The structure reveals how Rrn3 binding converts an inactive Pol I dimer into an initiation-competent monomeric complex and provides insights into the mechanisms of Pol I-specific initiation and regulation.
RNA polymerase I is the central enzyme that synthesizes ribosomal RNA in eukaryotic cells, and its regulation underlies cell growth. Here the authors present a high-resolution cryo-EM structure of the Pol I-Rrn3 complex that explains how Rrn3 specifically recognizes Pol I to form an initiation competent complex.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Enzymes
/ Humanities and Social Sciences
/ Pol1 Transcription Initiation Complex Proteins - chemistry
/ Pol1 Transcription Initiation Complex Proteins - genetics
/ Pol1 Transcription Initiation Complex Proteins - metabolism
/ RNA Polymerase I - chemistry
/ RNA Polymerase I - metabolism
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - metabolism
/ Science
/ Yeast
