Members of the RAD52 epistasis group are necessary for maintaining genomic integrity. Through homologous recombination (HR), RAD52 group proteins faithfully repair lesions caused by spontaneous or induced DNA damage. Two members of this group, Rad54 and Rdh54, are homologs and Swi/Snf-like ATPases with partially overlapping functions in vivo. Rad54 is thought to act during HR, during strand invasion and D-loop formation. Although Rdh54 has similar activity in vitro, its diploid-specific phenotype and role in checkpoint adaptation suggest additional functions for Rdh54. Localization of Rdh54 and Rad54 when fused to GFP tags has provided clues into the roles of these proteins in vivo. Rdh54 localizes constitutively to kinetochores and partially relocalizes to DNA repair foci post-DNA damage in both haploid and diploid cells, whereas Rad54 localizes solely to repair foci. These experiments aim to obtain clues into the function of Rdh54 from three approaches. Further study into the non-recombination functions of Rdh54 may reveal a role in the communication between the recombination process and the cellular components controlling chromosome segregation.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Predoctoral Individual National Research Service Award (F31)
Project #
1F31GM073567-01
Application #
6893556
Study Section
Special Emphasis Panel (ZRG1-F05 (29))
Program Officer
Gaillard, Shawn R
Project Start
2004-09-03
Project End
2008-09-02
Budget Start
2004-09-03
Budget End
2005-09-02
Support Year
1
Fiscal Year
2004
Total Cost
$32,798
Indirect Cost
Name
Columbia University (N.Y.)
Department
Genetics
Type
Schools of Medicine
DUNS #
621889815
City
New York
State
NY
Country
United States
Zip Code
10032
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Burgess, Rebecca C; Lisby, Michael; Altmannova, Veronika et al. (2009) Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo. J Cell Biol 185:969-81
Bernstein, Kara A; Shor, Erika; Sunjevaric, Ivana et al. (2009) Sgs1 function in the repair of DNA replication intermediates is separable from its role in homologous recombinational repair. EMBO J 28:915-25
Burgess, Rebecca C; Rahman, Sadia; Lisby, Michael et al. (2007) The Slx5-Slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination. Mol Cell Biol 27:6153-62