Homomeric interaction of the mouse Rad52 protein |
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Authors: | Krejci Lumir Thomsen Bo Duno Morten Westergaard Ole Bendixen Christian |
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Affiliation: | (1) Department of Animal Breeding and Genetics, Danish Institute of Agricultural Science, Research Centre Foulum, P.O. Box 50, DK-8830 Tjele, Denmark;(2) Department of Molecular & Structural Biology, University of Aarhus, DK-8000 Aarhus, Denmark |
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Abstract: | The Rad52 protein plays a crucial role in repairing DNA damage and homologous recombination, possibly by virtue of its ability to catalyze annealing of single-stranded DNA. In agreement with recent genetic data, we here present results based on the two-hybrid system, demonstrating that mouse Rad52p is able to form homomeric complexes. A small domain necessary and sufficient for the self-interaction is located in the conserved N-terminus of the protein. These data contribute to the important insights into the architecture of the multi-protein complex involved in recombinational DNA repair. |
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Keywords: | homo-dimerization RAD52 recombination repair two-hybrid system |
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