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KMID : 0380220070400030432
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Journal of Biochemistry and Molecular Biology
2007 Volume.40 No. 3 p.432 ~ p.438
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DNA-dependent Protein Kinase Mediates V(D)J Recombination via RAG2 Phosphorylation
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Hah Young-Sool
Lee Jung-Hwa
Kim Deok-Ryong
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Abstract
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V(D)J recombination, a site-specific gene rearrangement process occurring during the lymphocyte development, begins with DNA double strand breaks by two recombination activating gene products (RAG1/2) and finishes with the repair process by several proteins including DNA-dependent protein kinase (DNA-PK). In this report, we found that RAG2 was specifically phosphorylated by DNA-PK at the 365th serine residue, and this phosphorylated RAG2 affected the V(D)J recombination activity in cells in the GFP expression-based assay. While the V(D)J recombination activity between wild-type RAG2 and mutant S365A RAG2 in the assay using a signal joint substrate was undistinguishable in DNA-PK deficient cells (M059J), the activity with wild-type RAG2 was largely increased in DNA-PK proficient cells (M059K) in comparison with mutant RAG2, suggesting that RAG2 phosphorylation by DNA-PK plays a crucial role in the signal joint formation during V(D)J recombination.
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KEYWORD
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DNA-dependent protein kinase, Protein phosphorylation, Recombination activating gene 2, V(D)J recombination
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