Mol Cell. 2003 Aug;12(2):501-8.

C-terminal deletion of AID uncouples class switch recombination from somatic hypermutation and gene conversion.

Barreto V, Reina-San-Martin B, Ramiro AR, McBride KM, Nussenzweig MC.

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Laboratory of Molecular Immunology, The Rockefeller University, New York, NY 10021, USA.

Abstract

Class-switch recombination (CSR), somatic hypermutation (SHM), and antibody gene conversion are distinct DNA modification reactions, but all are initiated by activation-induced cytidine deaminase (AID), an enzyme that deaminates cytidine residues in single-stranded DNA. Here we describe a mutant form of AID that catalyzes SHM and gene conversion but not CSR. When expressed in E. coli, AID(delta189-198) is more active in catalyzing cytidine deamination than wild-type AID. AID(delta189-198) also promotes high levels of gene conversion and SHM when expressed in eukaryotic cells, but fails to induce CSR. These results underscore an essential role for the C-terminal domain of AID in CSR that is independent of its cytidine deaminase activity and that is not required for either gene conversion or SHM.

PMID:: 14536088; [PubMed - indexed for MEDLINE]

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Separate domains of AID are required for somatic hypermutation and class-switch recombination. [Nat Immunol. 2004]
Separate domains of AID are required for somatic hypermutation and class-switch recombination.
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C-terminal deletion of AID uncouples class switch recombination from somatic hypermutation and gene conversion.

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