{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yoon JH"],"funding":["National Institutes of Health","NIH HHS","NIGMS NIH HHS"],"pagination":["RP106934"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12408069"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14"],"pubmed_abstract":["Y-family DNA polymerases (Pols) are intrinsically highly error-prone; yet they conduct predominantly error-free translesion synthesis (TLS) in normal human cells. In response to DNA damage, Y-family Pols assemble and function together with WRN, WRNIP1, and Rev1 in TLS. Among these proteins, WRN possesses a 3'→5' exonuclease activity and an ATPase/3'→5' DNA helicase activity, and WRNIP1 has a DNA-dependent ATPase activity. In a previous study, we identified a role of WRN 3'→5' exonuclease activity in the high in vivo fidelity of TLS by Y-family Pols. Here we provide evidence for a crucial role of WRN and WRNIP1 ATPase activities in raising the fidelity of TLS by these Pols. Defects in WRN and WRNIP1 ATPase activities cause a diversity of nucleotide (nt) misincorporations opposite DNA lesion"],"journal":["eLife"],"pubmed_title":["WRN and WRNIP1 ATPases impose high fidelity on translesion synthesis by Y-family DNA polymerases."],"pmcid":["PMC12408069"],"funding_grant_id":["R35 GM148364"],"pubmed_authors":["Sellamuthu K","Prakash S","Yoon JH","Prakash L"],"additional_accession":[]},"is_claimable":false,"name":"WRN and WRNIP1 ATPases impose high fidelity on translesion synthesis by Y-family DNA polymerases.","description":"Y-family DNA polymerases (Pols) are intrinsically highly error-prone; yet they conduct predominantly error-free translesion synthesis (TLS) in normal human cells. In response to DNA damage, Y-family Pols assemble and function together with WRN, WRNIP1, and Rev1 in TLS. Among these proteins, WRN possesses a 3'→5' exonuclease activity and an ATPase/3'→5' DNA helicase activity, and WRNIP1 has a DNA-dependent ATPase activity. In a previous study, we identified a role of WRN 3'→5' exonuclease activity in the high in vivo fidelity of TLS by Y-family Pols. Here we provide evidence for a crucial role of WRN and WRNIP1 ATPase activities in raising the fidelity of TLS by these Pols. Defects in WRN and WRNIP1 ATPase activities cause a diversity of nucleotide (nt) misincorporations opposite DNA lesion","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-07-15T12:42:31.117Z","creation":"2026-07-04T03:16:08.154Z"},"accession":"S-EPMC12408069","cross_references":{"pubmed":["40900148"],"doi":["10.7554/eLife.106934"]}}