{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jia J"],"funding":["Deutsche Forschungsgemeinschaft","Alexander von Humboldt-Stiftung","Chinese Scholarship Council - PhD fellowship to J.J.","Georg-August-Universität Göttingen","Freie Universität Berlin"],"pagination":["5535"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7608686"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_abstract":["The ASCC3 subunit of the activating signal co-integrator complex is a dual-cassette Ski2-like nucleic acid helicase that provides single-stranded DNA for alkylation damage repair by the α-ketoglutarate-dependent dioxygenase AlkBH3. Other ASCC components integrate ASCC3/AlkBH3 into a complex DNA repair pathway. We mapped and structurally analyzed interacting ASCC2 and ASCC3 regions. The ASCC3 fragment comprises a central helical domain and terminal, extended arms that clasp the compact ASCC2 unit. ASCC2-ASCC3 interfaces are evolutionarily highly conserved and comprise a large number of residues affected by somatic cancer mutations. We quantified contributions of protein regions to the ASCC2-ASCC3 interaction, observing that changes found in cancers lead to reduced ASCC2-ASCC3 affinity. Func"],"journal":["Nature communications"],"pubmed_title":["The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations."],"pmcid":["PMC7608686"],"funding_grant_id":["BO3442/1-2","SFB860","FUB-QBI","Postdoctoral fellowship to A.J.P.B.","n.a."],"pubmed_authors":["Bohnsack KE","Hackert P","Absmeier E","Holton N","Wahl MC","Pietrzyk-Brzezinska AJ","Bohnsack MT","Jia J"],"additional_accession":[]},"is_claimable":false,"name":"The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations.","description":"The ASCC3 subunit of the activating signal co-integrator complex is a dual-cassette Ski2-like nucleic acid helicase that provides single-stranded DNA for alkylation damage repair by the α-ketoglutarate-dependent dioxygenase AlkBH3. Other ASCC components integrate ASCC3/AlkBH3 into a complex DNA repair pathway. We mapped and structurally analyzed interacting ASCC2 and ASCC3 regions. The ASCC3 fragment comprises a central helical domain and terminal, extended arms that clasp the compact ASCC2 unit. ASCC2-ASCC3 interfaces are evolutionarily highly conserved and comprise a large number of residues affected by somatic cancer mutations. We quantified contributions of protein regions to the ASCC2-ASCC3 interaction, observing that changes found in cancers lead to reduced ASCC2-ASCC3 affinity. Func","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Nov","modification":"2026-05-02T22:48:13.845Z","creation":"2020-11-19T16:59:52Z"},"accession":"S-EPMC7608686","cross_references":{"pubmed":["33139697"],"doi":["10.1038/s41467-020-19221-x"]}}