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Nuclear localization of Rad51B is independent of BRCA2

Journal Article · · Mutagenesis
Human Rad51 is critical for the maintenance of genome stability through its role in the repair of DNA double-strand breaks. Rad51B (Rad51L1/hRec2) is one of the five known paralogs of human Rad51 found in a multi-protein complex with three other Rad51 paralogs, Rad51C, Rad51D and Xrcc2. Examination of EGFP-Rad51B fusion protein in HeLa S3 cells and immunofluorescence in several human cell lines confirms the nuclear localization of Rad51B. This is the first report to detail putative interactions of a Rad51 paralog protein with BRCA2. Utilization of a BRCA2 mutant cell line, CAPAN-1 suggests that Rad51B localizes to the nucleus independent of BRCA2. Although both Rad51B and BRCA2 are clearly involved in the homologous recombinational repair pathway, Rad51B and BRCA2 do not appear to associate directly. Furthermore, mutations in the KKLK motif of Rad51B, amino acid residues 4-7, mislocalizes Rad51B to the cytoplasm suggesting that this is the nuclear localization signal for the Rad51B protein. Examination of wild-type EGFP-Rad51B fusion protein in mammalian cells deficient in Rad51C showed that Rad51B localizes to the nucleus independent of Rad51C; further suggesting that Rad51B, like Rad51C, contains its own nuclear localization signal.
Research Organization:
Lawrence Livermore National Laboratory (LLNL), Livermore, CA
Sponsoring Organization:
USDOE
DOE Contract Number:
W-7405-ENG-48
OSTI ID:
877911
Report Number(s):
UCRL-JRNL-213335
Journal Information:
Mutagenesis, Journal Name: Mutagenesis Journal Issue: 1 Vol. 20; ISSN MUTAEX; ISSN 0267-8357
Country of Publication:
United States
Language:
English

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