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• W2020107653 abstract "Affinity maturation and class switching of antibodies requires activation-induced cytidine deaminase (AID)-dependent hypermutation of Ig V(D)J rearrangements and Ig S regions, respectively, in activated B cells. AID deaminates deoxycytidine bases in Ig genes, converting them into deoxyuridines. In V(D)J regions, subsequent excision of the deaminated bases by uracil-DNA glycosylase, or by mismatch repair, leads to further point mutation or gene conversion, depending on the species. In Ig S regions, nicking at the abasic sites produced by AID and uracil-DNA glycosylases results in staggered double-strand breaks, whose repair by nonhomologous end joining mediates Ig class switching. We have tested whether nonhomologous end joining also plays a role in V(D)J hypermutation using chicken DT40 cells deficient for Ku70 or the DNA-dependent protein kinase catalytic subunit (DNA-PKcs). Inactivation of the Ku70 or DNA-PKcs genes in DT40 cells elevated the rate of AID-induced gene conversion as much as 5-fold. Furthermore, DNA-PKcs-deficiency appeared to reduce point mutation. The data provide strong evidence that double-strand DNA ends capable of recruiting the DNA-dependent protein kinase complex are important intermediates in Ig V gene conversion." @default.
• W2020107653 created "2016-06-24" @default.
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• W2020107653 date "2007-03-13" @default.
• W2020107653 modified "2023-10-01" @default.
• W2020107653 title "DNA-Dependent Protein Kinase Inhibits AID-Induced Antibody Gene Conversion" @default.
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• W2020107653 doi "https://doi.org/10.1371/journal.pbio.0050080" @default.
• W2020107653 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1820612" @default.
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