Skip Navigation


Mutagenesis Advance Access originally published online on February 8, 2005
Mutagenesis 2005 20(1):57-63; doi:10.1093/mutage/gei011
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
20/1/57    most recent
gei011v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (3)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Miller, K. A.
Right arrow Articles by Albala, J. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Miller, K. A.
Right arrow Articles by Albala, J. S.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?


Mutagenesis vol. 20 no. 1 © UK Environmental Mutagen Society 2005; all rights reserved.

Nuclear localization of Rad51B is independent of Rad51C and BRCA2

Kristi A. Miller, John M. Hinz, N.Alice Yamada, Lawrence H. Thompson and Joanna S. Albala*

Biology and Biotechnology Research Program, Lawrence Livermore National Laboratory, 7000 East Avenue, L-448, Livermore, CA 94550, USA

Rad51B is one of the five paralogs of human Rad51 and is found in a multiprotein complex with three other Rad51 paralogs, Rad51C, Rad51D and Xrcc2. Participation of Rad51B in this complex depends on its direct interaction with Rad51C. Examination of EGFP–Rad51B fusion protein in HeLa S3 cells and immunofluorescence in several human cell lines reveal the nuclear localization of Rad51B. Mutations in the N-terminal KKLK motif of Rad51B (amino acids 4–7), result in the cytoplasmic localization of Rad51B suggesting that the KKLK sequence is the nuclear localization signal (NLS) for the Rad51B protein. Examination of wild-type EGFP–Rad51B fusion protein in hamster irs3 mutant cells, deficient in Rad51C, showed that Rad51B localizes to the nucleus independently of Rad51C, the only known direct binding partner for Rad51B. Utilization of a BRCA2 mutant cell line, CAPAN-1, showed that Rad51B also 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. This study finds that a KKLK motif in the N-terminus of Rad51B serves as an NLS that allows Rad51B to localize to the nucleus independent of Rad51C or BRCA2.

* To whom correspondence should be addressed. Tel: +1 925 422 6442; Fax: +1 925 424 6605; Email: albala1{at}llnl.gov


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Nucleic Acids ResHome page
J.-Y. Park, H.-W. Yoo, B.-R. Kim, R. Park, S.-Y. Choi, and Y. Kim
Identification of a novel human Rad51 variant that promotes DNA strand exchange
Nucleic Acids Res., June 1, 2008; 36(10): 3226 - 3234.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.