A yeast protein analogous to Escherichia coli RecA protein whose cellular level is enhanced after UV irradiation.
In Saccharomyces cerevisiae, a protein was recognized by polyclonal antibodies raised against homogeneous Escherichia coli K 12 RecA protein. The cellular level of the yeast protein called RecAsc (molecular weight 44 kDa, pI 6.3), was transiently enhanced after UV irradiation. Protease inhibitors were required to minimize degradation of the RecAsc protein during cell lysis. The RecAsc protein exhibited similar basal levels and similar kinetics of increase after UV irradiation in DNA-repair proficient (RAD+) strains carrying mitochondrial DNA or not (rho0). This was also true for the following DNA-repair deficient (rad-) strains: rad2-6 rad6-1 rad52-1, a triple mutant blocked in three major repair pathways; rad6-delta, a mutant containing an integrative deletion in a gene playing a central role in mutagenesis; pso2-1, a mutant that exhibits a reduced rate of mutagenesis and recombination after exposure to DNA cross-linking agents.
D000906:Antibodies; D004307:Dose-Response Relationship, Radiation; D004926:Escherichia coli / Q000235:genetics*; D005838:Genotype; D007700:Kinetics; D011938:Rec A Recombinases / Q000528:radiation effects*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000528:radiation effects*; D013045:Species Specificity; D014466:Ultraviolet Rays
D000906:Antibodies; D011938:Rec A Recombinases