MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Krejci, L.
Right arrow Articles by Bendixen, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Krejci, L.
Right arrow Articles by Bendixen, C.

Molecular and Cellular Biology, February 2001, p. 966-976, Vol. 21, No. 3
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.3.966-976.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Molecular Dissection of Interactions between Rad51 and Members of the Recombination-Repair Group

Lumir Krejci,1,2 Jiri Damborsky,3 Bo Thomsen,2 Morten Duno,2 and Christian Bendixen2,*

Department of Analysis of Biologically Important Molecular Complexes, Masaryk University, 612 65 Brno,1 and Laboratory of Biomolecular Structure and Dynamics, Masaryk University, 611 37 Brno,3 Czech Republic, and Department of Breeding and Genetics, Section of Molecular Genetics, Research Center Foulum, DK-8830 Tjele, Denmark2

Received 11 September 2000/Returned for modification 10 October 2000/Accepted 26 October 2000

Recombination is important for the repair of DNA damage and for chromosome segregation during meiosis; it has also been shown to participate in the regulation of cell proliferation. In the yeast Saccharomyces cerevisiae, recombination requires products of the RAD52 epistasis group. The Rad51 protein associates with the Rad51, Rad52, Rad54, and Rad55 proteins to form a dynamic complex. We describe a new strategy to screen for mutations which cause specific disruption of the interaction between certain proteins in the complex, leaving other interactions intact. This approach defines distinct protein interaction domains and protein relationships within the Rad51 complex. Alignment of the mutations onto the constructed three-dimensional model of the Rad51 protein reveal possible partially overlapping interfaces for the Rad51-Rad52 and the Rad51-Rad54 interactions. Rad51-Rad55 and Rad51-Rad51 interactions are affected by the same spectrum of mutations, indicating similarity between the two modes of binding. Finally, the detection of a subset of mutations within Rad51 which disrupt the interaction with mutant Rad52 protein but activate the interaction with Rad54 suggests that dynamic changes within the Rad51 protein may contribute to an ordered reaction process.

* Corresponding author. Mailing address: Department of Breeding and Genetics, Section of Molecular Genetics, Research Center Foulum, P.O. Box 50, DK-8830 Tjele, Denmark. Phone: 45 89991360. Fax: 45 89991300. E-mail: Christian.Bendixen{at}agrsci.dk.

Molecular and Cellular Biology, February 2001, p. 966-976, Vol. 21, No. 3
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.3.966-976.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2001 by the American Society for Microbiology. All rights reserved.