Abstract
A full-length cDNA encoding the putative hepatic glycogen-binding (GL) subunit of protein phosphatase-1 (PP1) was isolated from a rat liver library. The deduced amino acid sequence (284 residues, 32.6 kDa) was 23% identical (39% similar) to the N-terminal region of the glycogen-binding (GM) subunit of PP1 from striated muscle. The similarities between GM and GL were most striking between residues 63-86, 144-166 and 186-227 of human GM (approximately 40% identity), nearly all the identities with the putative yeast homologue GAC1 being located between 144-166 and 186-227. The cDNA was expressed in E. coli, and the expressed protein transformed the properties of PP1 to those characteristic of the hepatic glycogen-associated enzyme. These experiments establish that the cloned protein is GL.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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Carrier Proteins / biosynthesis*
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism
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Cloning, Molecular
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DNA Primers
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Gene Library
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Glutathione Transferase / biosynthesis
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Humans
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Kinetics
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Liver / enzymology*
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Liver Glycogen / metabolism*
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Macromolecular Substances
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Molecular Sequence Data
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Muscle, Skeletal / enzymology*
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Open Reading Frames
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Organ Specificity
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Phosphoprotein Phosphatases / biosynthesis*
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Phosphoprotein Phosphatases / chemistry
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Phosphoprotein Phosphatases / metabolism
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Phosphorylase a / metabolism
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Polymerase Chain Reaction
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Protein Phosphatase 1
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Rabbits
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Rats
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Recombinant Fusion Proteins / metabolism
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Sequence Homology, Amino Acid
Substances
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Carrier Proteins
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DNA Primers
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Liver Glycogen
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Macromolecular Substances
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Recombinant Fusion Proteins
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Phosphorylase a
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Glutathione Transferase
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thiophosphorylase a
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Phosphoprotein Phosphatases
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Ppp1r3b protein, rat
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Protein Phosphatase 1