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J. Biol. Chem., Vol. 266, Issue 24, 15782-15789, Aug, 1991
PM Tang, JA Bondor, KM Swiderek and AA DePaoli-Roach
DNA clones encoding the glycogen-binding (RG1) subunit of glycogen-
associated protein phosphatase were isolated from rabbit skeletal muscle
lambda gt11 cDNA libraries. Overlapping clones provided an open reading
frame of 3327 nucleotides that predicts a polypeptide of 1109 amino acids
with a molecular weight of 124,257. Northern hybridization of rabbit RNA
identified a major mRNA transcript of 7.5 kilobases present in skeletal,
diaphragm, and cardiac muscle, but not in brain, kidney, liver, and lung.
Southern analysis of rabbit genomic DNA digested with various restriction
endonucleases gave rise to a single hybridizing fragment, suggesting that a
single gene is present. Expression of the complete RG1 subunit coding
sequence in Escherichia coli generated a protein of apparent molecular
weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis of
approximately 160,000, similar to the size of the polypeptide detected by
Western immunoblot in rabbit skeletal muscle extracts. The RG1 subunit
shares significant homology with the Saccharomyces cerevisiae GAC1 gene
product which is involved in activation of glycogen synthase and glycogen
accumulation. The homology with GAC1 substantiates the role of this enzyme
in control of glycogen metabolism. Hydropathy analysis of the RG1 subunit
amino acid sequence revealed the presence of a hydrophobic region in the
COOH terminus, suggesting a potential association with membrane. This
result suggests that the same phosphatase regulatory component may be
involved in targeting the enzyme both to membranes and to glycogen.
Molecular cloning and expression of the regulatory (RG1) subunit of the glycogen-associated protein phosphatase
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202-5122.
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