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Molecular and Cellular Biology, January 2006, p. 678-688, Vol. 26, No. 2
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.2.678-688.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Rec2 Interplay with both Brh2 and Rad51 Balances Recombinational Repair in Ustilago maydis

Milorad Kojic,1,{dagger} Qingwen Zhou,1,{dagger} Michael Lisby,2,{dagger} and William K. Holloman1*

Department of Microbiology and Immunology, Hearst Microbiology Research Center, 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 24 August 2005/ Returned for modification 28 September 2005/ Accepted 18 October 2005

Rec2 is the single Rad51 paralog in Ustilago maydis. Here, we find that Rec2 is required for radiation-induced Rad51 nuclear focus formation but that Rec2 foci form independently of Rad51 and Brh2. Brh2 foci also form in the absence of Rad51 and Rec2. By coprecipitation from cleared extracts prepared from Escherichia coli cells expressing the proteins, we found that Rec2 interacts physically not only with Rad51 and itself but also with Brh2. Transgenic expression of Brh2 in rec2 mutants can effectively restore radiation resistance, but the frequencies of spontaneous Rad51 focus formation and allelic recombination are elevated. The Dss1-independent Brh2-RPA70 fusion protein is also active in restoring radiation sensitivity of rec2 but is hyperactive to an extreme degree in allelic recombination and in suppressing the meiotic block of rec2. However, the high frequency of chromosome missegregation in meiotic products is an indicator of a corrupted process. The results demonstrate that the importance of Rec2 function is not only in stimulating recombination activity but also in ensuring that recombination is properly controlled.

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

{dagger} M.K., Q.Z., and M.L. contributed equally to this work.

Molecular and Cellular Biology, January 2006, p. 678-688, Vol. 26, No. 2
0022-538X/06/$08.00+0     doi:10.1128/MCB.26.2.678-688.2006
Copyright © 2006, 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]  
  • Zhou, Q., Kojic, M., Cao, Z., Lisby, M., Mazloum, N. A., Holloman, W. K. (2007). Dss1 Interaction with Brh2 as a Regulatory Mechanism for Recombinational Repair. Mol. Cell. Biol. 27: 2512-2526 [Abstract] [Full Text]  


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