Amino acid sequence and expression of the hepatic glycogen-binding (GL)-subunit of protein phosphatase-1

Autor: Martin J. Doherty, Patricia T.W. Cohen, Greg Moorhead, Philip Cohen, Nick Morrice
Rok vydání: 1995
Předmět:
Targetting subunit
Biochemistry
Polymerase Chain Reaction
chemistry.chemical_compound
Structural Biology
Protein Phosphatase 1
Phosphoprotein Phosphatases
Phosphorylase a
Cloning
Molecular
Peptide sequence
Glutathione Transferase
chemistry.chemical_classification
Glycogen
Protein phosphatase
Liver
Organ Specificity
Rabbits
Macromolecular Substances
Protein subunit
Recombinant Fusion Proteins
Phosphatase
Molecular Sequence Data
Biophysics
Biology
Open Reading Frames
Complementary DNA
Genetics
Animals
Humans
Amino Acid Sequence
Protein kinase A
Muscle
Skeletal
Molecular Biology
Cyclic AMP-dependent protein kinase
DNA Primers
Gene Library
Binding Sites
Base Sequence
Sequence Homology
Amino Acid
Protein phosphatase 1
Cell Biology
Molecular biology
Liver Glycogen
Rats
Kinetics
Enzyme
chemistry
Carrier Proteins
Glycogen metabolism
Zdroj: FEBS letters. 375(3)
ISSN: 0014-5793
Popis: 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.
Databáze: OpenAIRE
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