Modulation of RAG/DNA complex by HSP70 in V(D)J recombination

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초록

V(D)J recombination, a site-specific gene rearrangement process, requires two RAG1 and RAG2 proteins specifically recognizing recombination signal sequences and forming DNA double-strand breaks. The broken DNA ends tightly bound to RAG proteins are joined by repair proteins. Here, we found that heat shock protein 70 was associated with RAG2 following two-step affinity chromatography purification. It was also co-immunoprecipitated with RAG2 in pro-B cells. Purified HSP70 protein disrupted RAG/DNA complexes assembled in vitro and also inhibited the V(D)J cleavage (both nick and hairpin formation) in a dose-dependent manner. This HSP70 action required ATP energy. These data suggest that HSP70 might play a crucial role in disassembling RAG/DNA complexes stably formed during V(D)J recombination. (c) 2007 Elsevier Inc. All rights reserved.

키워드

V(D)J recombination; RAG2; HSP70; protein disassembling; SYNAPTIC COMPLEX; MU-TRANSPOSASE; RAG2 PROTEINS; DNA; CLEAVAGE; MECHANISM; CHAPERONE; RESIDUES
제목
Modulation of RAG/DNA complex by HSP70 in V(D)J recombination
저자
Son, Yong Mi; Lee, Jung Hwa; Kim, Deok Ryong
DOI
10.1016/j.bbrc.2007.10.132
발행일
2008-01
유형
Article
저널명
Biochemical and Biophysical Research Communications
권
365
호
1
페이지
113 ~ 117