期刊
NATURE
卷 502, 期 7473, 页码 644-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nature12636
关键词
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资金
- EMBL Heidelberg Protein Expression and Purification, Proteomics Core Facilities and Crystallization Platform
- 'Fermentation et culture de microorganisms' (CNRS) [IFR88]
- EMBO Long-Term fellowships
- Marie-Curie fellowship [FP7-PEOPLE-2011-IEF 301002]
- Fundacion Futuro fellowship
- ESF/CSIC
- Volkswagen Stiftung
- Spanish Ministry of Science [BFU2010-16336]
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 angstrom 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 alpha-amanitin. The A49-A34.5 heterodimer embraces subunit A135 through extended arms, thereby contacting and potentially regulating subunit A12.2.
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