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- Title
Key features of the interaction between Pcf11 CID and RNA polymerase II CTD.
- Authors
Noble, Christian G; Hollingworth, David; Martin, Stephen R; Ennis-Adeniran, Valerie; Smerdon, Stephen J; Kelly, Geoff; Taylor, Ian A; Ramos, Andres
- Abstract
The C-terminal domain (CTD) of the large subunit of RNA polymerase II is a platform for mRNA processing factors and links gene transcription to mRNA capping, splicing and polyadenylation. Pcf11, an essential component of the mRNA cleavage factor IA, contains a CTD-interaction domain that binds in a phospho-dependent manner to the heptad repeats within the RNA polymerase II CTD. We show here that the phosphorylated CTD exists as a dynamic disordered ensemble in solution and, by induced fit, it assumes a structured conformation when bound to Pcf11. In addition, we detected cis-trans populations for the CTD prolines, and found that only the all-trans form is selected for binding. These data suggest that the recognition of the CTD is regulated by independent site-specific modifications (phosphorylation and proline cis-trans isomerization) and, probably, by the local concentration of suitable binding sites.
- Publication
Nature structural & molecular biology, 2005, Vol 12, Issue 2, p144
- ISSN
1545-9993
- Publication type
Journal Article
- DOI
10.1038/nsmb887