激活诱导胞嘧啶脱氨酶（AID）的C末端缺失可使类别转换重组与体细胞高频突变及基因转换解偶联。
C-terminal deletion of AID uncouples class switch recombination from somatic hypermutation and gene conversion.
作者信息
Barreto Vasco, Reina-San-Martin Bernardo, Ramiro Almudena R, McBride Kevin M, Nussenzweig Michel C
机构信息
Laboratory of Molecular Immunology, The Rockefeller University, New York, NY 10021, USA.
出版信息
Mol Cell. 2003 Aug;12(2):501-8. doi: 10.1016/s1097-2765(03)00309-5.
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.
类别转换重组（CSR）、体细胞高频突变（SHM）和抗体基因转换是不同的DNA修饰反应，但它们均由活化诱导的胞嘧啶脱氨酶（AID）启动，AID是一种使单链DNA中的胞嘧啶残基脱氨的酶。在此，我们描述了一种AID突变形式，它催化SHM和基因转换，但不催化CSR。当在大肠杆菌中表达时，AID（δ189 - 198）在催化胞嘧啶脱氨方面比野生型AID更具活性。当在真核细胞中表达时，AID（δ189 - 198）也促进高水平的基因转换和SHM，但不能诱导CSR。这些结果强调了AID的C末端结构域在CSR中的重要作用，该作用独立于其胞嘧啶脱氨酶活性，并且基因转换或SHM均不需要该结构域。
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