Three human RNA polymerases interact with TFIIH via a common RPB6 subunit

Masahiko Okuda, Tetsufumi Suwa, Hidefumi Suzuki, Yuki Yamaguchi, and Yoshifumi Nishimura

Nucleic Acids Research, gkab612, doi:10.1093/nar/gkab612

RPB6, a common subunit shared by all three eukaryotic RNA polymerases (RNAPI, RNAPII, and RNAPIII) contains a short N-terminal tail (NTT) of so far unknown function. Here, we have revealed that NTT interacts with the PH domain (PH-D) of the p62 subunit of the general transcription/repair factor TFIIH, and solved structures of RPB6 in its free and complexed forms with PH-D by NMR. Using available cryo-EM structures, the authors have modelled the activated elongation complex of RNAPII bound to TFIIH. In addition, the authors provide evidence that the p62-RPB6 interaction plays multiple roles in transcription, transcription-coupled nucleotide excision repair, and cell proliferation, suggesting that TFIIH is engaged in all RNA polymerase systems.

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