Communication between distant sites in RNA polymerase II through ubiquitylation factors and the polymerase CTD Journal Article
| Authors: | Somesh, B. P.; Sigurdsson, S.; Saeki, H.; Erdjument-Bromage, H.; Tempst, P.; Svejstrup, J. Q. |
| Article Title: | Communication between distant sites in RNA polymerase II through ubiquitylation factors and the polymerase CTD |
| Abstract: | Transcriptional 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. © 2007 Elsevier Inc. All rights reserved. |
| Keywords: | controlled study; unclassified drug; sequence analysis; nonhuman; ubiquitin; protein domain; dna damage; ubiquitin protein ligase; carboxy terminal sequence; protein protein interaction; ubiquitination; amino acid sequence; molecular sequence data; saccharomyces cerevisiae; models, molecular; dimerization; mutagenesis, site-directed; protein structure, tertiary; binding sites; saccharomyces cerevisiae proteins; protein subunit; protein folding; ubiquitin protein ligase e3; enzyme specificity; enzyme binding; enzyme subunit; ubiquitin-conjugating enzymes; rna polymerase ii; enzyme mechanism; enzyme modification; ubiquitin protein ligase e2; ubiquitin-protein ligase complexes |
| Journal Title: | Cell |
| Volume: | 129 |
| Issue: | 1 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 2007-04-06 |
| Start Page: | 57 |
| End Page: | 68 |
| Language: | English |
| DOI: | 10.1016/j.cell.2007.01.046 |
| PUBMED: | 17418786 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 22" - "Export Date: 17 November 2011" - "CODEN: CELLB" - "Source: Scopus" |
