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7DTH

Solution structure of RPB6, common subunit of RNA polymerases I, II, and III

Summary for 7DTH
Entry DOI10.2210/pdb7dth/pdb
NMR InformationBMRB: 36405
DescriptorDNA-directed RNA polymerases I, II, and III subunit RPABC2 (1 entity in total)
Functional Keywordsrna polymerase, nuclear protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight14773.31
Authors
Okuda, M.,Nishimura, Y. (deposition date: 2021-01-05, release date: 2022-01-19, Last modification date: 2024-05-15)
Primary citationOkuda, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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