PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23798704-7 2013 Interestingly, a hybrid protein containing the N-terminal region of Rad54, responsible for Rad51 interaction, fused to the Swi2/Snf2 core of Rdh54 is able to effectively complement the sensitivity to both methyl methanesulfonate and excess Rad51 in rdh54 null cells. Methyl Methanesulfonate 205-228 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 68-73 27001511-7 2016 Regulation of HR by NMD extends to multiple targets beyond RAD55, including RAD51, RAD54 and RAD57 Finally, we demonstrate that loss of NMD results in an increase in recombination rates and resistance to the DNA damaging agent methyl methanesulfonate, suggesting this pathway negatively regulates HR under normal growth conditions. Methyl Methanesulfonate 227-250 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 83-88 17671161-3 2007 Here, we have identified a specific role for the Shu proteins in a Rad51/Rad54-dependent HRR pathway(s) to repair MMS-induced lesions during S-phase. Methyl Methanesulfonate 114-117 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 73-78 18430956-7 2008 This gene, with close sequence similarity to RAD54, complements methylmethane sulfonate (MMS) sensitivity but not UV sensitivity or gene targeting defects of rad54Delta mutant yeast cells. Methyl Methanesulfonate 64-87 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 45-50 18430956-7 2008 This gene, with close sequence similarity to RAD54, complements methylmethane sulfonate (MMS) sensitivity but not UV sensitivity or gene targeting defects of rad54Delta mutant yeast cells. Methyl Methanesulfonate 89-92 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 45-50 17671161-4 2007 We show that, although mutation of RAD51 or RAD54 prevented the formation of MMS-induced HRR intermediates (X-molecules) arising during replication in sgs1 cells, mutation of SHU genes attenuated the level of these structures. Methyl Methanesulfonate 77-80 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 44-49 12087154-4 2002 Mutations in the Rad54 ATPase domain (ATPase(-)) impair Rad54 function in vitro, sensitize yeast to killing by methylmethane sulfonate and reduce spontaneous gene conversion. Methyl Methanesulfonate 111-134 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 17-22 12172964-4 2002 RAD54 and RNR2 reporter activity in response to the DNA damaging agent, methyl methanesulphonate, was measured in ddc1-Delta, rad9-Delta, ddc1-Delta/rad9-Delta, dun1-Delta, crt1-Delta and mbp1-Delta mutants and was compared with that of the wild type. Methyl Methanesulfonate 72-96 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 0-5 11292336-4 2001 In vivo, GST-Rad54 protein carried out the functions required for methyl methanesulfonate sulfate (MMS), UV, and DSB repair. Methyl Methanesulfonate 99-102 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 13-18 8805304-10 1996 The hHR54 cDNA could partially complement the methyl methanesulfonate-sensitive phenotype of S. cerevisiae rad54 delta cells. Methyl Methanesulfonate 46-69 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 107-112 9171366-5 1997 Strikingly, overexpression of Rad54p can functionally suppress the UV and methyl methanesulfonate sensitivity caused by a deletion of the RAD51 gene. Methyl Methanesulfonate 74-97 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 30-36 9409819-4 1997 However, the rdh54 null mutation enhances the methyl methanesulfonate sensitivity of a rad54 mutant and single rdh54 mutants are sensitive to prolonged exposure at high concentrations of methyl methanesulfonate. Methyl Methanesulfonate 46-69 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 87-92 9409820-4 1997 The rad54 mutant is sensitive to the alkylating agent, methyl methanesulfonate (MMS), and is defective in interchromosomal and intrachromosomal gene conversion. Methyl Methanesulfonate 55-78 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 4-9 9409820-4 1997 The rad54 mutant is sensitive to the alkylating agent, methyl methanesulfonate (MMS), and is defective in interchromosomal and intrachromosomal gene conversion. Methyl Methanesulfonate 80-83 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 4-9 9409820-6 1997 However, the rad54 rdh54/tid1 mutant is more sensitive to MMS and more defective in interchromosomal gene conversion than is the rad54 mutant, but shows the same frequency of intrachromosomal gene conversion as the rad54 mutant. Methyl Methanesulfonate 58-61 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 13-18 3550429-5 1987 In addition, the RAD54 gene fusion was inducible in both haploid and diploid cells in response to the DNA-damaging agents X-rays, UV light, and methyl methanesulfonate, but not in response to heat shock. Methyl Methanesulfonate 144-167 DNA-dependent ATPase RAD54 Saccharomyces cerevisiae S288C 17-22