Dynamic conformational switching underlies TFIIH function in transcription and DNA repair and impacts genetic diseases

Yu, Jina; Yan, Chunli; Dodd, Thomas; Tsai, Chi-Lin; Tainer, John A.; Tsutakawa, Susan E.; Ivanov, Ivaylo

doi:10.1038/s41467-023-38416-6

Dynamic conformational switching underlies TFIIH function in transcription and DNA repair and impacts genetic diseases

Journal Article · Sat May 13 00:00:00 EDT 2023 · Nature Communications

DOI:https://doi.org/10.1038/s41467-023-38416-6· OSTI ID:2229304

^[1]; Yan, Chunli ^[1]; Dodd, Thomas ^[1]; Tsai, Chi-Lin ^[2]; Tainer, John A. ^[3]; Tsutakawa, Susan E. ^[4]; ^[1]

Georgia State University, Atlanta, GA (United States)
The University of Texas MD Anderson Cancer Center, Houston, TX (United States)
The University of Texas MD Anderson Cancer Center, Houston, TX (United States); Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Transcription factor IIH (TFIIH) is a protein assembly essential for transcription initiation and nucleotide excision repair (NER). Yet, understanding of the conformational switching underpinning these diverse TFIIH functions remains fragmentary. TFIIH mechanisms critically depend on two translocase subunits, XPB and XPD. To unravel their functions and regulation, we build cryo-EM based TFIIH models in transcription- and NER-competent states. Using simulations and graph-theoretical analysis methods, we reveal TFIIH’s global motions, define TFIIH partitioning into dynamic communities and show how TFIIH reshapes itself and self-regulates depending on functional context. Our study uncovers an internal regulatory mechanism that switches XPB and XPD activities making them mutually exclusive between NER and transcription initiation. By sequentially coordinating the XPB and XPD DNA-unwinding activities, the switch ensures precise DNA incision in NER. Mapping TFIIH disease mutations onto network models reveals clustering into distinct mechanistic classes, affecting translocase functions, protein interactions and interface dynamics.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities (SUF); National Institutes of Health (NIH); National Science Foundation (NSF)

Grant/Contract Number:: AC02-05CH11231; AC05-00OR22725

OSTI ID:: 2229304

Journal Information:: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 14; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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