PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8939806-5 1996 We found that cells carrying rad6, rad18, rad50 and rad52 single mutations are far more sensitive to killing by MMS than the mag1 mutant, that double mutants were much more sensitive than either of the corresponding single mutants, and that the effects of the double mutants were either additive or synergistic, suggesting that post-replication and recombination-repair pathways recognize either the same lesions as MAG1 and APN1, or else some differ- ent lesions produced by MMS treatment. Methyl Methanesulfonate 112-115 recombinase RAD52 Saccharomyces cerevisiae S288C 52-57 24163251-7 2014 The phenylalanine-349 and tyrosine-409 residues present in the C-terminal half of Rad52 were critical for the interaction with Rad51, the disruption of Rad51 oligomers, the mediator activity of the full-length protein and for DNA repair in vivo in the presence of methyl methanesulfonate. Methyl Methanesulfonate 264-287 recombinase RAD52 Saccharomyces cerevisiae S288C 82-87 23328489-5 2013 Therefore, we expressed the wild-type BRCA2 in yeast and determined the effect of BRCA2 on yeast homologous recombination, methyl methanesulphonate (MMS)-induced Rad51 and Rad52 foci and MMS sensitivity. Methyl Methanesulfonate 123-147 recombinase RAD52 Saccharomyces cerevisiae S288C 172-177 23328489-5 2013 Therefore, we expressed the wild-type BRCA2 in yeast and determined the effect of BRCA2 on yeast homologous recombination, methyl methanesulphonate (MMS)-induced Rad51 and Rad52 foci and MMS sensitivity. Methyl Methanesulfonate 149-152 recombinase RAD52 Saccharomyces cerevisiae S288C 172-177 15010319-6 2004 The rad52 smc6-56 double mutant showed a sensitivity to MMS similar to that of the rad52 single mutant, indicating that Smc6 is involved in a pathway that requires Rad52 to function. Methyl Methanesulfonate 56-59 recombinase RAD52 Saccharomyces cerevisiae S288C 4-9 11810260-5 2002 rad52 Delta is epistatic to mms1 Delta for MMS and camptothecin sensitivity, indicating that Mms1 acts in concert with Rad52. Methyl Methanesulfonate 43-46 recombinase RAD52 Saccharomyces cerevisiae S288C 0-5 10511548-1 1999 C-terminal rad52 truncation and internal deletion mutants were characterized for their ability to repair MMS-induced double-strand breaks and to produce viable spores during meiosis. Methyl Methanesulfonate 105-108 recombinase RAD52 Saccharomyces cerevisiae S288C 11-16 22025679-5 2012 We demonstrate that, after exposure to MMS, H3K56ac-deficient cells cannot complete DNA replication and eventually segregate chromosomes with intranuclear foci containing the recombination protein Rad52. Methyl Methanesulfonate 39-42 recombinase RAD52 Saccharomyces cerevisiae S288C 197-202 18310075-7 2008 Accordingly, expression of a protein species that harbors the middle and C-terminal regions of Rad52 in the rad52 Delta327 background enhances the association of Rad51 protein with a HO-made DNA double-strand break and partially complements the methylmethane sulfonate sensitivity of the mutant cells. Methyl Methanesulfonate 245-268 recombinase RAD52 Saccharomyces cerevisiae S288C 95-100 18310075-7 2008 Accordingly, expression of a protein species that harbors the middle and C-terminal regions of Rad52 in the rad52 Delta327 background enhances the association of Rad51 protein with a HO-made DNA double-strand break and partially complements the methylmethane sulfonate sensitivity of the mutant cells. Methyl Methanesulfonate 245-268 recombinase RAD52 Saccharomyces cerevisiae S288C 108-113 11212925-3 2001 In this study, we found that SGS1 forms part of the RAD52 epistasis group when cells are exposed to MMS. Methyl Methanesulfonate 100-103 recombinase RAD52 Saccharomyces cerevisiae S288C 52-57 8765159-4 1996 Additional experiments revealed that yeast RAD52 gene expression increased the level of resistance to the DNA damaging agents diepoxybutane, and methyl methanesulfonate, but did not alter sensitivity to ultraviolet radiation. Methyl Methanesulfonate 145-168 recombinase RAD52 Saccharomyces cerevisiae S288C 43-48 7982574-1 1994 We have screened for mutations of the Saccharomyces cerevisiae RAD52 gene which confer a temperature-sensitive (ts) phenotype with respect to either the repair of DNA lesions caused by methyl methanesulfonate (MMS) or the recombination of an intrachromosomal recombination reporter. Methyl Methanesulfonate 185-208 recombinase RAD52 Saccharomyces cerevisiae S288C 63-68 7982574-1 1994 We have screened for mutations of the Saccharomyces cerevisiae RAD52 gene which confer a temperature-sensitive (ts) phenotype with respect to either the repair of DNA lesions caused by methyl methanesulfonate (MMS) or the recombination of an intrachromosomal recombination reporter. Methyl Methanesulfonate 210-213 recombinase RAD52 Saccharomyces cerevisiae S288C 63-68 6098821-1 1984 The RAD52 gene of Saccharomyces cerevisiae, which is involved in genetic recombination and DNA repair, was cloned by transformation of rad52-1 mutant cells to methyl methanesulfonate resistance with BamHI fragments of Rad+ genomic DNA inserted into the Escherichia coli-S. cerevisiae shuttle vector YRp7. Methyl Methanesulfonate 159-182 recombinase RAD52 Saccharomyces cerevisiae S288C 4-9 6098821-2 1984 A plasmid carrying a 2.0-kilobase BamHI fragment was found to partially complement methyl methanesulfonate sensitivity of the rad52-1 mutant. Methyl Methanesulfonate 83-106 recombinase RAD52 Saccharomyces cerevisiae S288C 126-131