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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.
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