Communication between Distant Sites in RNA Polymerase II through Ubiquitylation Factors and the Polymerase CTD
| Autor: | Jesper Q. Svejstrup, Paul Tempst, Hideaki Saeki, Baggavalli P. Somesh, Stefan Sigurdsson, Hediye Erdjument-Bromage |
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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Saccharomyces cerevisiae Proteins Molecular Sequence Data RNA polymerase II Saccharomyces cerevisiae Biology medicine.disease_cause General Biochemistry Genetics and Molecular Biology Protein structure Ubiquitin medicine Amino Acid Sequence Binding site Peptide sequence Polymerase Genetics Mutation Binding Sites Endosomal Sorting Complexes Required for Transport Biochemistry Genetics and Molecular Biology(all) Mutagenesis Ubiquitin-Protein Ligase Complexes Protein Structure Tertiary Cell biology Ubiquitin-Conjugating Enzymes Mutagenesis Site-Directed biology.protein RNA Polymerase II Dimerization DNA Damage |
| Zdroj: | Cell. 129:57-68 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/j.cell.2007.01.046 |
| Popis: | SummaryTranscriptional arrest triggers ubiquitylation of RNA polymerase II (RNAPII). We mapped the yeast RNAPII ubiquitylation sites and found that they play an important role in elongation and the DNA-damage response. One site lies in a protein domain that is unordered in free RNAPII, but ordered in the elongating form, helping explain the preferential ubiquitylation of this form. The other site is >125 Ångstroms away, yet mutation of either site affects ubiquitylation of the other, in vitro and in vivo. The basis for this remarkable coupling was uncovered: an Rsp5 (E3) dimer assembled on the RNAPII C-terminal domain (CTD). The ubiquitylation sites bind Ubc5 (E2), which in turn binds Rsp5 to allow modification. Evidence for folding of the CTD compatible with this mechanism of communication between distant sites is provided. These data reveal the specificity and mechanism of RNAPII ubiquitylation and demonstrate that E2s can play a crucial role in substrate recognition. |
| Databáze: | OpenAIRE |
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