Crystal structure of the 14-subunit RNA polymerase I
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | Nature |
Volume | 502 |
Issue number | 7473 |
Pages (from-to) | 644-9 |
Number of pages | 6 |
ISSN | 0028-0836 |
DOIs | |
Publication status | Published - 2013 |
Externally published | Yes |
- Catalytic Domain, Crystallography, X-Ray, DNA/chemistry, Models, Molecular, Peptide Chain Elongation, Translational, Protein Binding, Protein Conformation, Protein Multimerization, Protein Subunits/chemistry, RNA Polymerase I/chemistry, RNA Polymerase II/chemistry, RNA Polymerase III/chemistry, Saccharomyces cerevisiae/enzymology, Transcription, Genetic
Research areas
ID: 194520972