TY - JOUR
T1 - Rad22 protein, a Rad52 homologue in Schizosaccharomyces pombe, binds to DNA double-strand breaks
AU - Kim, Woo Jae
AU - Lee, Suman
AU - Park, Min Sung
AU - Jang, Yeun Kyu
AU - Kim, Jae Bum
AU - Park, Sang Dai
PY - 2000/11/10
Y1 - 2000/11/10
N2 - DNA double-strand breaks can be introduced by exogenous agents or during normal cellular processes. Genes belonging to the RAD52 eplstasis group are known to repair these breaks in budding yeast. Among these genes, RAD52 plays a central role in homologous recombination and DNA double-strand break repair. Despite its importance, its mechanism of action is not yet clear. It is known, however, that the human homologue of Rad52 is capable of binding to DNA ends in vitro. Herein, we show that Rad22 protein, a Rad52 homologue in the fission yeast Schizosaccharomyces pombe, can similarly bind to DNA ends at double-strand breaks. This end-binding ability was demonstrated in vitro by electron microscopy and by protection from exonuclease attack. We also showed that Rad22 specifically binds near double-strand break associated with mating type switching in vivo by chromatin immunoprecipitation analysis. This is the first evidence that a recombinational protein directly binds to DNA double-strand breaks in vivo.
AB - DNA double-strand breaks can be introduced by exogenous agents or during normal cellular processes. Genes belonging to the RAD52 eplstasis group are known to repair these breaks in budding yeast. Among these genes, RAD52 plays a central role in homologous recombination and DNA double-strand break repair. Despite its importance, its mechanism of action is not yet clear. It is known, however, that the human homologue of Rad52 is capable of binding to DNA ends in vitro. Herein, we show that Rad22 protein, a Rad52 homologue in the fission yeast Schizosaccharomyces pombe, can similarly bind to DNA ends at double-strand breaks. This end-binding ability was demonstrated in vitro by electron microscopy and by protection from exonuclease attack. We also showed that Rad22 specifically binds near double-strand break associated with mating type switching in vivo by chromatin immunoprecipitation analysis. This is the first evidence that a recombinational protein directly binds to DNA double-strand breaks in vivo.
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U2 - 10.1074/jbc.M007060200
DO - 10.1074/jbc.M007060200
M3 - Article
C2 - 10956666
AN - SCOPUS:0034634685
SN - 0021-9258
VL - 275
SP - 35607
EP - 35611
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 45
ER -