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Papers In Press, published online ahead of print November 6, 2006
J. Biol. Chem, 10.1074/jbc.M607439200
Submitted on August 4, 2006
Revised on October 24, 2006
Accepted on November 6, 2006

Requirement of non-canonical activity of uracil DNA glycosylase for class switch recombination

Nasim Ara Begum, Nakako Izumi, Momoko Nishikori, Hitoshi Nagaoka, Reiko Shinkura, and Tasuku Honjo

Immunology and Genomic Medicine, Kyoto University Graduate School of Medicine, Kyoto 606-8501

Corresponding Author: honjo{at}mfour.med.kyoto-u.ac.jp

Activation-induced cytidine deaminase (AID) and uracil DNA glycosylase (UNG) are required for class switch recombination (CSR). AID is involved in the DNA cleavage step of CSR, but the precise role of UNG is not yet understood. Mutations and deletions are footprints of abortive DNA cleavage in the immunoglobulin switch region in splenic B cells stimulated to undergo CSR. However, a UNG deficiency did not reduce the number of such footprints, indicating UNG is dispensable for the DNA cleavage step. Mutagenesis experiments revealed that UNG's role in CSR depends on its WXXF motif. This motif is also essential for UNG's interaction with the HIV viral peptide Vpr, which recruits UNG to the HIV particle. Furthermore, exogenous Vpr had a dominant-negative effect on CSR. These results suggest that UNG is recruited to the CSR machinery through its WXXF motif by a Vpr-like host factor and plays a novel noncanonical role in a CSR step that follows DNA cleavage.


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