7DTI

Solution structure of the complex between RNA polymerase subunit RPB6 and TFIIH p62 PH domain

Summary for 7DTI

• Entry DOI: 10.2210/pdb7dti/pdb
• NMR Information: BMRB: 36406
• Descriptor: DNA-directed RNA polymerases I, II, and III subunit RPABC2, General transcription factor IIH subunit 1 (2 entities in total)
• Functional Keywords: rna polymerase, general transcription factor, nuclear protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 27361.90

Authors

Okuda, M.,Nishimura, Y. (deposition date: 2021-01-05, release date: 2022-08-10, Last modification date: 2024-05-15)

Primary citation

Okuda, M.,Suwa, T.,Suzuki, H.,Yamaguchi, Y.,Nishimura, Y.
Three human RNA polymerases interact with TFIIH via a common RPB6 subunit.
Nucleic Acids Res., 50:1-16, 2022

PubMed Abstract: In eukaryotes, three RNA polymerases (RNAPs) play essential roles in the synthesis of various types of RNA: namely, RNAPI for rRNA; RNAPII for mRNA and most snRNAs; and RNAPIII for tRNA and other small RNAs. All three RNAPs possess a short flexible tail derived from their common subunit RPB6. However, the function of this shared N-terminal tail (NTT) is not clear. Here we show that NTT interacts with the PH domain (PH-D) of the p62 subunit of the general transcription/repair factor TFIIH, and present the structures of RPB6 unbound and bound to PH-D by nuclear magnetic resonance (NMR). Using available cryo-EM structures, we modelled the activated elongation complex of RNAPII bound to TFIIH. We also provide evidence that the recruitment of TFIIH to transcription sites through the p62-RPB6 interaction is a common mechanism for transcription-coupled nucleotide excision repair (TC-NER) of RNAPI- and RNAPII-transcribed genes. Moreover, point mutations in the RPB6 NTT cause a significant reduction in transcription of RNAPI-, RNAPII- and RNAPIII-transcribed genes. These and other results show that the p62-RPB6 interaction plays multiple roles in transcription, TC-NER, and cell proliferation, suggesting that TFIIH is engaged in all RNAP systems.

PubMed: 34268577
DOI: 10.1093/nar/gkab612

Experimental method

SOLUTION NMR