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Molecular and Cellular Biology, April 2007, p. 2512-2526, Vol. 27, No. 7
0270-7306/07/$08.00+0     doi:10.1128/MCB.01907-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Dss1 Interaction with Brh2 as a Regulatory Mechanism for Recombinational Repair{triangledown}

Qingwen Zhou,1,{dagger} Milorad Kojic,1,{dagger} Zhimin Cao,1 Michael Lisby,2 Nayef A. Mazloum,1 and William K. Holloman1*

Department of Microbiology and Immunology, Cornell University Weill Medical College, New York, New York 10021,1 Department of Genetics, Institute of Molecular Biology, University of Copenhagen, Øster Farimagsgade 2A, DK-1353 Copenhagen, Denmark2

Received 9 October 2006/ Returned for modification 2 November 2006/ Accepted 17 January 2007

Brh2, the BRCA2 ortholog in Ustilago maydis, enables recombinational repair of DNA by controlling Rad51 and is in turn regulated by Dss1. Interplay with Rad51 is conducted via the BRC element located in the N-terminal region of the protein and through an unrelated domain, CRE, at the C terminus. Mutation in either BRC or CRE severely reduces functional activity, but repair deficiency of the brh2 mutant can be complemented by expressing BRC and CRE on different molecules. This intermolecular complementation is dependent upon the presence of Dss1. Brh2 molecules associate through the region overlapping with the Dss1-interacting domain to form at least dimer-sized complexes, which in turn, can be dissociated by Dss1 to monomer. We propose that cooperation between BRC and CRE domains and the Dss1-provoked dissociation of Brh2 complexes are requisite features of Brh2's molecular mechanism.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Box 62, Cornell University Weill Medical College, 1300 York Ave., New York, NY 10021. Phone: (212) 746-6510. Fax: (212) 746-8587. E-mail: wkhollo{at}med.cornell.edu.

{triangledown} Published ahead of print on 29 January 2007.

{dagger} The first two authors contributed equally to this work.

Molecular and Cellular Biology, April 2007, p. 2512-2526, Vol. 27, No. 7
0270-7306/07/$08.00+0     doi:10.1128/MCB.01907-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Zhou, Q., Kojic, M., Holloman, W. K. (2009). DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA. J. Biol. Chem. 284: 8265-8273 [Abstract] [Full Text]  
  • Mazloum, N., Zhou, Q., Holloman, W. K. (2008). D-loop formation by Brh2 protein of Ustilago maydis. Proc. Natl. Acad. Sci. USA 105: 524-529 [Abstract] [Full Text]  


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