Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

The RNA polymerase II (RNAPII) C-terminal domain (CTD) heptapeptide repeats (1-YSPTSPS-7) undergo dynamic phosphorylation and dephosphorylation during the transcription cycle to recruit factors that regulate transcription, RNA processing and chromatin modification. We show here that RPRD1A and RPRD1B form homodimers and heterodimers through their coiled-coil domains and interact preferentially via CTD-interaction domains (CIDs) with RNAPII CTD repeats phosphorylated at S2 and S7. Crystal structures of the RPRD1A, RPRD1B and RPRD2 CIDs, alone and in complex with RNAPII CTD phosphoisoforms, elucidate the molecular basis of CTD recognition. In an example of cross-talk between different CTD modifications, our data also indicate that RPRD1A and RPRD1B associate directly with RPAP2 phosphatase and, by interacting with CTD repeats where phospho-S2 and/or phospho-S7 bracket a phospho-S5 residue, serve as CTD scaffolds to coordinate the dephosphorylation of phospho-S5 by RPAP2.

Original publication

DOI

10.1038/nsmb.2853

Type

Journal article

Journal

Nat Struct Mol Biol

Publication Date

08/2014

Volume

21

Pages

686 - 695

Keywords

Amino Acid Sequence, Amino Acid Substitution, Carrier Proteins, Cell Cycle Proteins, Crystallography, X-Ray, HEK293 Cells, Humans, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Neoplasm Proteins, Phosphorylation, Protein Binding, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Processing, Post-Translational, Protein Structure, Quaternary, Protein Structure, Secondary, RNA Polymerase II, Repressor Proteins, Serine