2026-04-13T00:38:08Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/1243842025-12-05T12:03:28Zcom_2072_1057col_2072_478916col_2072_478917

00925njm 22002777a 4500 dc Rodríguez Cortez, Virginia Carolina author Martínez Redondo, Paloma author Català Moll, Francesc author Rodríguez Ubreva, Javier author García Gómez, Antonio author Poorani Subramani, Ganesh author Ciudad, Laura author Hernando, Henar author Pérez García, Arantxa author Company, Carlos author Urquiza, José M. author Ramiro, Almudena R. author Noia, Javier M. Di author Vaquero García, Alejandro author Ballestar Tarín, Esteban author 2018-09-10T07:22:44Z 2018-09-10T07:22:44Z 2017-08-08 2018-07-24T12:02:38Z Activation-induced cytidine deaminase (AID) triggers antibody diversification in B cells by catalysing deamination and subsequently mutating immunoglobulin (Ig) genes. Association of AID with RNA Pol II and occurrence of epigenetic changes during Ig gene diversification suggest participation of AID in epigenetic regulation. AID is mutated in hyper-IgM type 2 (HIGM2) syndrome. Here, we investigated the potential role of AID in the acquisition of epigenetic changes. We discovered that AID binding to the IgH locus promotes an increase in H4K20me3. In 293F cells, we demonstrate interaction between co-transfected AID and the three SUV4-20 histone H4K20 methyltransferases, and that SUV4-20H1.2, bound to the IgH switch (S) mu site, is replaced by SUV4-20H2 upon AID binding. Analysis of HIGM2 mutants shows that the AID truncated form W68X is impaired to interact with SUV4-20H1.2 and SUV4-20H2 and is unable to bind and target H4K20me3 to the Smu site. We finally show in mouse primary B cells undergoing class-switch recombination (CSR) that AID deficiency associates with decreased H4K20me3 levels at the Smu site. Our results provide a novel link between SUV4-20 enzymes and CSR and offer a new aspect of the interplay between AID and histone modifications in setting the epigenetic status of CSR sites. RNA Epigenètica Epigenetics Activation-induced cytidine deaminase targets SUV4-20-mediated histone H4K20 trimethylation to class-switch recombination sites