被撤回的出版物: Identification of a specific domain required for dimerization of activation-induced cytidine deaminase (Retracted Article. See vol 283, pg 660, 2008)

Activation-induced cytidine deaminase (AID) is essential to all three genetic alterations required for generation of antigen-specific immunoglobulin: class switch recombination, somatic hypermutation, and gene conversion. Here we demonstrate that AID molecules form a homodimer autonomously in the absence of RNA, DNA, other cofactors, or post-translational modifications. Studies on serial deletion mutants revealed the minimum region between Thr(27) and His(56) responsible for dimerization. Analyses of point mutations within this region revealed that the residues between Gly(47) and Gly(54) are most important for the dimer formation. Functional analyses of these mutations indicate that all mutations impairing the dimer formation are inefficient for class switching, suggesting that dimer formation is required for class switching activity. Dimer formation and its requirement for the function of AID are features that AID shares with APOBEC-1, an RNAediting enzyme of apolipoprotein B100 mRNA.