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J Biol Chem, Vol. 273, Issue 16, 9644-9650, April 17, 1998
From the Department of Molecular and Cellular Biology, Harvard
University, Cambridge, Massachusetts 02138
The yeast Saccharomyces cerevisiae
Sgs1 protein is a member of a family of DNA helicases that include the
Escherichia coli RecQ protein and the products of human
Bloom's syndrome and Werner's syndrome genes. To study the enzymatic
characteristics of the protein, a recombinant Sgs1 fragment (amino
acids 400-1268 of the 1447-amino acid full-length protein) was
overexpressed in yeast and purified to near homogeneity. The purified
protein exhibits an ATPase activity in the presence of single- or
double-stranded DNA. In the presence of ATP or dATP, unwinding of
duplex DNA or a DNA-RNA heteroduplex by the recombinant Sgs1 fragment
was readily observed. Similar to the E. coli RecQ helicase,
displacement of the DNA strand occurs in the 3' to 5' direction with
respect to the single-stranded DNA flanking the duplex. The efficiency
of unwinding was found to correlate inversely with the length of the
duplex region and was enhanced by the presence of E. coli single-stranded DNA-binding protein. In addition, the recombinant Sgs1
fragment was found to bind more tightly to a forked DNA substrate than
to either single- or double-stranded DNA.
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R. J. Bennett and J. C. Wang Association of yeast DNA topoisomerase III and Sgs1 DNA helicase: Studies of fusion proteins PNAS, September 25, 2001; 98(20): 11108 - 11113. [Abstract] [Full Text] [PDF]
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