Title |
Crystal structure of the 14-subunit RNA polymerase I
|
---|---|
Published in |
Nature, October 2013
|
DOI | 10.1038/nature12636 |
Pubmed ID | |
Authors |
Carlos Fernández-Tornero, María Moreno-Morcillo, Umar J. Rashid, Nicholas M. I. Taylor, Federico M. Ruiz, Tim Gruene, Pierre Legrand, Ulrich Steuerwald, Christoph W. Müller |
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. |
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