{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shimada K"],"funding":["Novartis Research Foundation","Swiss National Science Foundation","Swiss Cancer League"],"pagination":["e202101138"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8321694"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4(9)"],"pubmed_abstract":["DNA polymerase δ, which contains the catalytic subunit, Pol3, Pol31, and Pol32, contributes both to DNA replication and repair. The deletion of pol31 is lethal, and compromising the Pol3-Pol31 interaction domains confers hypersensitivity to cold, hydroxyurea (HU), and methyl methanesulfonate, phenocopying pol32Δ. We have identified alanine-substitutions in pol31 that suppress these deficiencies in pol32Δ cells. We characterize two mutants, pol31-T415A and pol31-W417A, which map to a solvent-exposed loop that mediates Pol31-Pol3 and Pol31-Rev3 interactions. The pol31-T415A substitution compromises binding to the Pol3 CysB domain, whereas Pol31-W417A improves it. Importantly, loss of Pol32, such as pol31-T415A, leads to reduced Pol3 and Pol31 protein levels, which are restored by pol31-W417A"],"journal":["Life science alliance"],"pubmed_title":["The stabilized Pol31-Pol3 interface counteracts Pol32 ablation with differential effects on repair."],"pmcid":["PMC8321694"],"funding_grant_id":["4167-02-2017","31003A-176286","176286"],"pubmed_authors":["Vijeh Motlagh ND","Gut H","Tsai-Pflugfelder M","Fuchs J","Gasser SM","Delgoshaie N","Shimada K"],"additional_accession":[]},"is_claimable":false,"name":"The stabilized Pol31-Pol3 interface counteracts Pol32 ablation with differential effects on repair.","description":"DNA polymerase δ, which contains the catalytic subunit, Pol3, Pol31, and Pol32, contributes both to DNA replication and repair. The deletion of pol31 is lethal, and compromising the Pol3-Pol31 interaction domains confers hypersensitivity to cold, hydroxyurea (HU), and methyl methanesulfonate, phenocopying pol32Δ. We have identified alanine-substitutions in pol31 that suppress these deficiencies in pol32Δ cells. We characterize two mutants, pol31-T415A and pol31-W417A, which map to a solvent-exposed loop that mediates Pol31-Pol3 and Pol31-Rev3 interactions. The pol31-T415A substitution compromises binding to the Pol3 CysB domain, whereas Pol31-W417A improves it. Importantly, loss of Pol32, such as pol31-T415A, leads to reduced Pol3 and Pol31 protein levels, which are restored by pol31-W417A","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Sep","modification":"2025-05-31T23:33:28.155Z","creation":"2025-05-31T23:33:28.155Z"},"accession":"S-EPMC8321694","cross_references":{"pubmed":["34226278"],"doi":["10.26508/lsa.202101138"]}}