{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Faustino AM"],"funding":["Sloan Foundation","Camille and Henry Dreyfus Foundation","Ada Sinz Hill fellowship","Howard Hughes Medical Institute","NSF Graduate Research Fellowship","Alfred P. Sloan Foundation","National Institute of General Medical Sciences","NIGMS NIH HHS","National Science Foundation"],"pagination":["e70237"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12679948"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["34(8)"],"pubmed_abstract":["Monoubiquitinated histone H2B at K123 in yeast (K120 in humans) is a transient modification that is both attached and removed during transcription. H2B is ubiquitinated in yeast by the E2/E3 pair, Rad6/Bre1, and deubiquitinated by two enzymes, Ubp8 and Ubp10. Previous studies had shown that Ubp10 has higher activity on ubiquitinated H2A/H2B dimers than on intact nucleosomes, but that activity on nucleosomes is higher in the presence of the histone chaperone, FACT. By contrast, the Ubp8 complex has equal activity on both histone substrates and is unaffected by FACT. We report here the results of single-molecule FRET experiments showing that FACT unwraps DNA and evicts ubiquitinated H2A/H2B dimers, the preferred substrate of Ubp10. To explore the basis for the differing activity of Ubp10 on "],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["An intrinsically disordered region of Ubp10 regulates its binding and activity on ubiquitinated histone substrates."],"pmcid":["PMC12679948"],"funding_grant_id":["DP2 GM140926","R35‐GM122569","R35-GM130393","DP2-GM140926","R35 GM122569","T32 GM008403","F32 GM128299","R35‐GM130393","DP2‐GM140926","R35-GM122569","MCB2045844","R35 GM130393"],"pubmed_authors":["Manriquez-Sandoval E","Poyton M","Nune M","Faustino AM","Wolberger C","Fried SD","Merino-Urteaga R","Ha T"],"additional_accession":[]},"is_claimable":false,"name":"An intrinsically disordered region of Ubp10 regulates its binding and activity on ubiquitinated histone substrates.","description":"Monoubiquitinated histone H2B at K123 in yeast (K120 in humans) is a transient modification that is both attached and removed during transcription. H2B is ubiquitinated in yeast by the E2/E3 pair, Rad6/Bre1, and deubiquitinated by two enzymes, Ubp8 and Ubp10. Previous studies had shown that Ubp10 has higher activity on ubiquitinated H2A/H2B dimers than on intact nucleosomes, but that activity on nucleosomes is higher in the presence of the histone chaperone, FACT. By contrast, the Ubp8 complex has equal activity on both histone substrates and is unaffected by FACT. We report here the results of single-molecule FRET experiments showing that FACT unwraps DNA and evicts ubiquitinated H2A/H2B dimers, the preferred substrate of Ubp10. To explore the basis for the differing activity of Ubp10 on ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-06-06T00:12:21.611Z","creation":"2026-05-23T03:13:58.176Z"},"accession":"S-EPMC12679948","cross_references":{"pubmed":["40716115"],"doi":["10.1002/pro.70237"]}}