%0 Journal Article %T Rad51 ATP binding but not hydrolysis is required to recruit Rad10 in synthesis-dependent strand annealing sites in <i>S. cerevisiae</i> %A Justin Karlin %A Paula L. Fischhaber %J Advances in Biological Chemistry %P 295-303 %@ 2162-2191 %D 2013 %I Scientific Research Publishing %R 10.4236/abc.2013.33033 %X
Several modes of eukaryotic of DNA double strand break repair (DSBR) depend on synapsis of complementary DNA. The Rad51 ATPase, the S. cerevisiae homolog of E. coli RecA, plays a key role in this process by catalyzing homology searching and strand exchange between an invading DNA strand and a repair template (e.g. sister chromatid or homologous chromosome). Synthesis dependent strand annealing (SDSA), a mode of DSBR, requires Rad51. Another repair enzyme, the Rad1-Rad10 endonuclease, acts in the final stages of SDSA, hydrolyzing 3бщ overhanging single-stranded DNA. Here we show in vivo by fluo-rescence microscopy that the ATP binding function of yeast Rad51 is required to recruit Rad10 SDSA sites indicating that Rad51 pre-synaptic filament formation must occur prior to the recruitment of Rad1-Rad10. Our data also show that Rad51 ATPase activity, an important step in Rad51 filament disassembly, is not absolutely required in order to recruit Rad1- Rad10 to DSB sites.
%K Rad1 %K Rad10 %K Rad51 %K Synthesis Dependent Strand Annealing %K Yeast %K Double Strand Break Repair %U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=33565