RPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds for Ser5 dephosphorylation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2014-08

AUTHORS

Zuyao Ni, Chao Xu, Xinghua Guo, Gerald O Hunter, Olga V Kuznetsova, Wolfram Tempel, Edyta Marcon, Guoqing Zhong, Hongbo Guo, Wei-Hung William Kuo, Joyce Li, Peter Young, Jonathan B Olsen, Cuihong Wan, Peter Loppnau, Majida El Bakkouri, Guillermo A Senisterra, Hao He, Haiming Huang, Sachdev S Sidhu, Andrew Emili, Shona Murphy, Amber L Mosley, Cheryl H Arrowsmith, Jinrong Min, Jack F Greenblatt

ABSTRACT

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. More... »

PAGES

686-695

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.2853

DOI

http://dx.doi.org/10.1038/nsmb.2853

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022363225

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24997600


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