{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Selvam K"],"funding":["U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences","U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS)","NIEHS NIH HHS","U.S. Department of Health & Human Services | NIH | National Institute of Environmental Health Sciences","U.S. Department of Health & Human Services | NIH | National Institute of Environmental Health Sciences (NIEHS)","NIGMS NIH HHS"],"pagination":["6223"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11266705"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_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."],"journal":["Nature communications"],"pubmed_title":["Elf1 promotes transcription-coupled repair in yeast by using its C-terminal domain to bind TFIIH."],"pmcid":["PMC11266705"],"funding_grant_id":["R01 ES028698","R21 ES035139","R01GM102362","R01ES028698","R01ES032814","R21ES035139","R01 ES032814","R01 GM102362"],"pubmed_authors":["Oh J","Wang D","Wyrick JJ","Li Q","Selvam K","Xu J","Wilson HE"],"additional_accession":[]},"is_claimable":false,"name":"Elf1 promotes transcription-coupled repair in yeast by using its C-terminal domain to bind TFIIH.","description":"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.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-02T22:59:53.658Z","creation":"2025-04-19T13:11:25.853Z"},"accession":"S-EPMC11266705","cross_references":{"pubmed":["39043658"],"doi":["10.1038/s41467-024-50539-y"]}}