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Volume 271, Number 43, Issue of October 25, 1996 pp. 26554-26560
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Initiation of Glycogen Synthesis in Yeast
REQUIREMENT OF MULTIPLE TYROSINE RESIDUES FOR FUNCTION OF THE SELF-GLUCOSYLATING Glg PROTEINS IN VIVO

(Received for publication, April 1, 1996, and in revised form, June 17, 1996)

From the Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202

The self-glucosylating proteins, Glg1p and Glg2p, are required for glycogen synthesis in Saccharomyces cerevisiae (Cheng, C., Mu., J., Farkas, I., Huang, D., Goebl M. G., and Roach, P. J. (1995) Mol. Cell. Biol. 15, 6632-6640). Glg2p was shown to be associated with carbohydrate in vivo and was released from the high molecular weight glycogen fraction by treatment with -amylase. In addition, some Glg2p exists as a protein of M_r ~43,000, whose proportion is increased in cells lacking glycogen synthase. Unlike the mammalian counterpart, glycogenin, the yeast Glg proteins appear to require multiple Tyr residues for functionality. In Glg2p, mutation of both Tyr²³⁰ and Tyr²³² is necessary to suppress self-glucosylation of purified protein in vitro. The mutant protein is still capable of transferring glucose to an exogeneous acceptor, n-dodecyl -D-maltoside. A small COOH-terminal region, conserved between Glg1p and Glg2p, is also important for function; mutation of Tyr³⁶⁷ or truncation at residue 362 impairs the ability of primed Glg2p to be elongated by glycogen synthase. Complete suppression of glycogen accumulation in vivo requires mutation of all three Tyr residues. In Glg1p, two Tyr residues are implicated, Tyr²³² and Tyr⁶⁰⁰, mutation of both being required to eliminate glycogen accumulation in vivo.

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