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- Title
Crystal structure of the 14-subunit RNA polymerase I.
- Authors
Fernández-Tornero, Carlos; Moreno-Morcillo, María; Rashid, Umar J.; Taylor, Nicholas M. I.; Ruiz, Federico M.; Gruene, Tim; Legrand, Pierre; Steuerwald, Ulrich; Müller, Christoph W.
- 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.
- Subjects
RNA polymerases; CRYSTAL structure; PROTEIN synthesis; CELL growth; BACTERIAL enzymes; SACCHAROMYCES cerevisiae; EUKARYOTES
- Publication
Nature, 2013, Vol 502, Issue 7473, p644
- ISSN
0028-0836
- Publication type
Article
- DOI
10.1038/nature12636