TY - JOUR
T1 - Rad10 exhibits lesion-dependent genetic requirements for recruitment to DNA double-strand breaks in Saccharomyces cerevisiae
AU - Moore, Destaye M.
AU - Karlin, Justin
AU - González-Barrera, Sergio
AU - Mardiros, Armen
AU - Lisby, Michael
AU - Doughty, Ana
AU - Gilley, Jennifer
AU - Rothstein, Rodney
AU - Friedberg, Errol C.
AU - Fischhaber, Paula L.
N1 - Funding Information:
California State University Northridge’s Competition for Research, Scholarship and Creative Activity Awards [to P.L.F.], the National Institutes of Health [5-R01-ES011344 to E.C.F., SC2GM081155 to P.L.F., GM50237, GM67055 to R.R.], the Danish Agency for Science, Technology and Innovation [to M.L.], the Villum Kann Rasmussen Foundation [to M.L.] and Fundación Alfonso Martín Escudero [to S.G.-B.]. Funding for open access charge: National Institutes of Health (SC2GM081155).
PY - 2009
Y1 - 2009
N2 - In the yeast Saccharomyces cerevisiae , the Rad1-Rad10 protein complex participates in nucleotide excision repair (NER) and homologous recombination (HR). During HR, the Rad1-Rad10 endonuclease cleaves 3′ branches of DNA and aberrant 3′ DNA ends that are refractory to other 3′ processing enzymes. Here we show that yeast strains expressing fluorescently labeled Rad10 protein (Rad10-YFP) form foci in response to double-strand breaks (DSBs) induced by a site-specific restriction enzyme, I- Sce I or by ionizing radiation (IR). Additionally, for endonuclease-induced DSBs, Rad10-YFP localization to DSB sites depends on both RAD51 and RAD52 , but not MRE11 while IR-induced breaks do not require RAD51. Finally, Rad10-YFP colocalizes with Rad51-CFP and with Rad52-CFP at DSB sites, indicating a temporal overlap of Rad52, Rad51 and Rad10 functions at DSBs. These observations are consistent with a putative role of Rad10 protein in excising overhanging DNA ends after homology searching and refine the potential role(s) of the Rad1-Rad10 complex in DSB repair in yeast.
AB - In the yeast Saccharomyces cerevisiae , the Rad1-Rad10 protein complex participates in nucleotide excision repair (NER) and homologous recombination (HR). During HR, the Rad1-Rad10 endonuclease cleaves 3′ branches of DNA and aberrant 3′ DNA ends that are refractory to other 3′ processing enzymes. Here we show that yeast strains expressing fluorescently labeled Rad10 protein (Rad10-YFP) form foci in response to double-strand breaks (DSBs) induced by a site-specific restriction enzyme, I- Sce I or by ionizing radiation (IR). Additionally, for endonuclease-induced DSBs, Rad10-YFP localization to DSB sites depends on both RAD51 and RAD52 , but not MRE11 while IR-induced breaks do not require RAD51. Finally, Rad10-YFP colocalizes with Rad51-CFP and with Rad52-CFP at DSB sites, indicating a temporal overlap of Rad52, Rad51 and Rad10 functions at DSBs. These observations are consistent with a putative role of Rad10 protein in excising overhanging DNA ends after homology searching and refine the potential role(s) of the Rad1-Rad10 complex in DSB repair in yeast.
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U2 - 10.1093/nar/gkp709
DO - 10.1093/nar/gkp709
M3 - Article
C2 - 19729509
AN - SCOPUS:71049127354
SN - 0305-1048
VL - 37
SP - 6429
EP - 6438
JO - Nucleic acids research
JF - Nucleic acids research
IS - 19
ER -