Activation-induced cytidine deaminase structure and functions: a species comparative view |
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| Authors: | Barreto Vasco M Magor Brad G |
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| Affiliation: | a Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6 P-2780-156 Oeiras, Portugal
b Department of Biological Sciences, University of Alberta, CW-405 Bioscience Building, Edmonton, AB T6G 2E5, Canada |
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| Abstract: | In the ten years since the discovery of activation-induced cytidine deaminase (AID) there has been considerable effort to understand the mechanisms behind this enzyme's ability to target and modify immunoglobulin genes leading to somatic hypermutation and class switch recombination. While the majority of research has focused on mouse and human models of AID function, work on other species, from lamprey to rabbit and sheep, has taught us much about the scope of functions of the AID mutator. This review takes a species-comparative approach to what has been learned about the AID mutator enzyme and its role in humoral immunity. |
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| Keywords: | Aag, alkyladenine DNA glycosylase APE1, apurinic/apyrimidinic endonuclease 1 APOBEC, Apolipoprotein B mRNA-editing enzyme catalytic BAC, bacterial artificial chromosome BER, base excision repair CIT, CD40L, IL-4 and TGF-βcocktail CDR, complementarity determining region CSR, class switch recombination DNA-PKcs, DNA-dependent protein kinase catalytic subunit DSB, double strand break HEL, hen egg lysozyme HIGM2, Hyper IgM type 2 IGC, Ig gene conversion miRNA or miR-#, microRNA MMR, mismatch repair NES, nuclear export signal NHEJ, non-homologous end joining NLS, nuclear localization signal NTS, non-transcribed strand PCNA, proliferating cell nuclear antigen PKA, protein kinase A PmCDA, Petromyzon marinus cytidine deaminase RPA, replication protein A SHM, somatic hypermutation TS, transcribed strand UNG, uracil-N-glycosylase VLR, variable lymphocyte receptor |
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