Download MendeleyKey Features of the Interaction between Pcf11 Cid and RNA Polymerase II Ctd.
Noble, C.G., Hollingworth, D., Martin, S.R., Adeniran, V.E., Smerdon, S.J., Kelly, G., Taylor, I.A., Ramos, A.(2005) Nat Struct Mol Biol 12: 144
- PubMed: 15665873
- DOI: https://doi.org/10.1038/nsmb887
- Primary Citation of Related Structures:
2BF0 - PubMed 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.
Organizational Affiliation:
Division of Protein Structure, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.
