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Title: | Crystal structure of the 14-subunit RNA polymerase I |
Authors: | Fernández-Tornero, Carlos ![]() ![]() |
Keywords: | Conformational flexibility Transcription initiation Electron-microscopy Elongation complex Phase information Cross-linking Architecture Subunits Model TFIIF |
Issue Date: | 31-Oct-2013 |
Publisher: | Springer Nature |
Citation: | Nature 502 (7473) 644–649 (2013) |
Abstract: | Protein biosynthesis depends on the availability of ribosomes, which in turn relies on ribosomal RNA production. In eukaryotes, this process is carried out by RNA polymerase I (Pol I), a 14-subunit enzyme, the activity of which is a major determinant of cell growth. Here we present the crystal structure of Pol I from Saccharomyces cerevisiae at 3.0 Å resolution. The Pol I structure shows a compact core with a wide DNA-binding cleft and a tightly anchored stalk. An extended loop mimics the DNA backbone in the cleft and may be involved in regulating Pol I transcription. Subunit A12.2 extends from the A190 jaw to the active site and inserts a transcription elongation factor TFIIS-like zinc ribbon into the nucleotide triphosphate entry pore, providing insight into the role of A12.2 in RNA cleavage and Pol I insensitivity to α-amanitin. The A49–A34.5 heterodimer embraces subunit A135 through extended arms, thereby contacting and potentially regulating subunit A12.2. |
Description: | 16 p.-5 fig.-8 extend. dat. fig.-1 extend. dat. tab. |
Publisher version (URL): | https://doi.org/10.1038/nature12636 |
URI: | http://hdl.handle.net/10261/212378 |
DOI: | http://dx.doi.org/10.1038/nature12636 |
ISSN: | 0028-0836 |
E-ISSN: | 1476-4687 |
Appears in Collections: | (CIB) Artículos |
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