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

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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Ni Z,Xu C,Guo X,Hunter GO,Kuznetsova OV,Tempel W,Marcon E,Zhong G,Guo H,Kuo WW,Li J,Young P,Olsen JB,Wan C,Loppnau P,El Bakkouri M,Senisterra GA,He H,Huang H,Sidhu SS,Emili A,Murphy S,Mosley AL,Arrowsmith CH

doi

10.1038/nsmb.2853

subject

Has Abstract

pub_date

2014-08-01 00:00:00

pages

686-695

issue

8

eissn

1545-9993

issn

1545-9985

journal_volume

21

pub_type

杂志文章

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