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J. Biol. Chem., Vol. 266, Issue 24, 15602-15607, 08, 1991
I Farkas, TA Hardy, MG Goebl and PJ Roach
In previous work, we identified a Saccharomyces cerevisiae glycogen
synthase gene, GSY1, which codes for an 85-kDa polypeptide present in
purified yeast glycogen synthase (Farkas, I., Hardy, T.A., DePaoli- Roach,
A.A., and Roach, P.J. (1990) J. Biol. Chem. 265, 20879-20886). We have now
cloned another gene, GSY2, which encodes a second S. cerevisiae glycogen
synthase. The GSY2 sequence predicts a protein of 704 residues, molecular
weight 79,963, with 80% identity to the protein encoded by GSY1. Amino acid
sequences obtained from a second polypeptide of 77 kDa present in yeast
glycogen synthase preparations matched those predicted by GSY2. GSY1
resides on chromosome VI, and GSY2 is located on chromosome XII. Disruption
of the GSY1 gene produced a strain retaining about 85% of wild type
glycogen synthase activity at stationary phase, while disruption of the
GSY2 gene yielded a strain with only about 10% of wild type enzyme
activity. The level of glycogen synthase activity in yeast cells disrupted
for GSY1 increased in stationary phase, whereas the activity remained at a
constant low level in cells disrupted for GSY2. Disruption of both genes
resulted in a viable haploid that totally lacked glycogen synthase activity
and was defective in glycogen deposition. In conclusion, yeast expresses
two forms of glycogen synthase with activity levels that behave differently
in the growth cycle. The GSY2 gene product appears to be the predominant
glycogen synthase with activity linked to nutrient depletion.
Two glycogen synthase isoforms in Saccharomyces cerevisiae are coded by distinct genes that are differentially controlled
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202-5122.
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