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J. Biol. Chem., Vol. 281, Issue 28, 19115-19123, July 14, 2006

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Identification of a Specific Domain Required for Dimerization of Activation-induced Cytidine Deaminase^*

From the Department of Immunology and Genomic Medicine, Graduate School of Medicine, Kyoto University, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan

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 Thr²⁷ and His⁵⁶ responsible for dimerization. Analyses of point mutations within this region revealed that the residues between Gly⁴⁷ and Gly⁵⁴ 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 RNA editing enzyme of apolipoprotein B100 mRNA.

Received for publication, February 21, 2006 , and in revised form, April 6, 2006.

^* This work was supported by Center of Excellence Grant 12CE2006 from the Ministry of Education, Science, Sports, and Culture of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Tel.: 81-75-753-4371; Fax: 81-75-753-9485; E-mail: honjo{at}mfour.med.kyoto-u.ac.jp.

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