DNA-dependent protein kinase mediates V(D)J recombination via RAG2 phosphorylation
- Authors
- Hah, Young-Sool; Lee, Jung Hwa; Kim, Deok Ryong
- Issue Date
- 31-May-2007
- Publisher
- SPRINGER SINGAPORE PTE LTD
- Keywords
- dNA-dependent protein kinase; protein phosphorylation; recombination activating gene 2; V(D)J recombination
- Citation
- JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.40, no.3, pp.432 - 438
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY
- Volume
- 40
- Number
- 3
- Start Page
- 432
- End Page
- 438
- URI
- https://scholarworks.bwise.kr/gnu/handle/sw.gnu/28375
- ISSN
- 1225-8687
- Abstract
- 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 365(th) 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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