The Saccharomyces cerevisiae Sgs1 protein, together with Schizosaccharomyce
s pombe Rqh1 and the human Bloom and Werner proteins, is a DNA helicase of
the Escherichia coli RecQ family. Mutation of SGS1 causes premature aging i
n yeast cells, including the accumulation of extrachromosomal rDNA circles.
We have recently shown that Sgs1p interacts with the DNA repair Rad16p pro
tein and is epistatic to Rad16p for UVC, 4-NQO and H2O2 lesions. Therefore
we tested sgs1 strains containing mutations in the helicase and C-terminal
domains. We demonstrate here that the helicase activity of the Sgs1 is impo
rtant for most elements of the sgs1 mutation phenotype, including sensitivi
ty to UVC, 4-NQO, H2O2, MMS and hydroxyurea.