{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen F"],"funding":["Natural Science Foundation of Tianjin City","Fundamental Research Funds for the Central Universities, Nankai University","National Natural Science Foundation of China"],"pagination":["e2025291118"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8379938"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["118(33)"],"pubmed_abstract":["The highly conserved multifunctional polymerase-associated factor 1 (Paf1) complex (PAF1C), composed of five core subunits Paf1, Leo1, Ctr9, Cdc73, and Rtf1, participates in all stages of transcription and is required for the Rad6/Bre1-mediated monoubiquitination of histone H2B (H2Bub). However, the molecular mechanisms underlying the contributions of the PAF1C subunits to H2Bub are not fully understood. Here, we report that Ctr9, acting as a hub, interacts with the carboxyl-terminal acidic tail of Rad6, which is required for PAF1C-induced stimulation of H2Bub. Importantly, we found that the Ras-like domain of Cdc73 has the potential to accelerate ubiquitin discharge from Rad6 and thus facilitates H2Bub, a process that might be conserved from yeast to humans. Moreover, we found that Rtf1 H"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination."],"pmcid":["PMC8379938"],"funding_grant_id":["31870750","030/63211052","20JCYBJC01320","31670758"],"pubmed_authors":["Guo L","Long J","Ge X","Chen F","Feng W","Liu B","Li DF","Zhou H"],"additional_accession":[]},"is_claimable":false,"name":"Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination.","description":"The highly conserved multifunctional polymerase-associated factor 1 (Paf1) complex (PAF1C), composed of five core subunits Paf1, Leo1, Ctr9, Cdc73, and Rtf1, participates in all stages of transcription and is required for the Rad6/Bre1-mediated monoubiquitination of histone H2B (H2Bub). However, the molecular mechanisms underlying the contributions of the PAF1C subunits to H2Bub are not fully understood. Here, we report that Ctr9, acting as a hub, interacts with the carboxyl-terminal acidic tail of Rad6, which is required for PAF1C-induced stimulation of H2Bub. Importantly, we found that the Ras-like domain of Cdc73 has the potential to accelerate ubiquitin discharge from Rad6 and thus facilitates H2Bub, a process that might be conserved from yeast to humans. Moreover, we found that Rtf1 H","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Aug","modification":"2025-04-05T14:05:41.5Z","creation":"2025-04-05T14:05:41.5Z"},"accession":"S-EPMC8379938","cross_references":{"pubmed":["34385316"],"doi":["10.1073/pnas.2025291118"]}}