Elf1 promotes transcription-coupled repair in yeast by using its C-terminal domain to bind TFIIH

Kathiresan Selvam, Jun Xu, Hannah E. Wilson, Juntaek Oh, Qingrong Li, Dong Wang () and John J. Wyrick ()
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Kathiresan Selvam: Washington State University
Jun Xu: University of California San Diego
Hannah E. Wilson: Washington State University
Juntaek Oh: University of California San Diego
Qingrong Li: University of California San Diego
Dong Wang: University of California San Diego
John J. Wyrick: Washington State University

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract Transcription coupled-nucleotide excision repair (TC-NER) removes DNA lesions that block RNA polymerase II (Pol II) transcription. A key step in TC-NER is the recruitment of the TFIIH complex, which initiates DNA unwinding and damage verification; however, the mechanism by which TFIIH is recruited during TC-NER, particularly in yeast, remains unclear. Here, we show that the C-terminal domain (CTD) of elongation factor-1 (Elf1) plays a critical role in TC-NER in yeast by binding TFIIH. Analysis of genome-wide repair of UV-induced cyclobutane pyrimidine dimers (CPDs) using CPD-seq indicates that the Elf1 CTD in yeast is required for efficient TC-NER. We show that the Elf1 CTD binds to the pleckstrin homology (PH) domain of the p62 subunit of TFIIH in vitro, and identify a putative TFIIH-interaction region (TIR) in the Elf1 CTD that is important for PH binding and TC-NER. The Elf1 TIR shows functional, structural, and sequence similarities to a conserved TIR in the mammalian UV sensitivity syndrome A (UVSSA) protein, which recruits TFIIH during TC-NER in mammalian cells. These findings suggest that the Elf1 CTD acts as a functional counterpart to mammalian UVSSA in TC-NER by recruiting TFIIH in response to Pol II stalling at DNA lesions.

Date: 2024
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DOI: 10.1038/s41467-024-50539-y

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