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

AI Article Synopsis

  • - The C-terminal domain (CTD) of RNA polymerase II (RNAPII) features heptapeptide repeats that change their phosphorylation state during transcription, impacting overall gene regulation and RNA processing.
  • - RPRD1A and RPRD1B proteins can form homodimers or heterodimers and prefer to bind with specific phosphorylated CTD repeats on RNAPII.
  • - RPRD1A and RPRD1B also interact with the RPAP2 phosphatase, coordinating the removal of a specific phosphorylation mark (S5) on the CTD, showcasing interaction between different phosphorylation states.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4124035PMC
http://dx.doi.org/10.1038/nsmb.2853DOI Listing

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