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

First Author  Son YM Year  2008
Journal  Biochem Biophys Res Commun Volume  365
Issue  1 Pages  113-7
PubMed ID  17980153 Mgi Jnum  J:128511
Mgi Id  MGI:3767363 Doi  10.1016/j.bbrc.2007.10.132
Citation  Son YM, et al. (2008) Modulation of RAG/DNA complex by HSP70 in V(D)J recombination. Biochem Biophys Res Commun 365(1):113-7
abstractText  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.
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