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Amino acid sequence and expression of the hepatic glycogen‐binding (G L ‐subunit of protein phosphatase‐1
Author(s) -
Doherty Martin J.,
Moorhead Greg,
Morrice Nick,
Cohen Philip,
Cohen Patricia T.W.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01184-g
Subject(s) - protein phosphatase 1 , complementary dna , protein subunit , biology , microbiology and biotechnology , peptide sequence , phosphatase , cdna library , amino acid , glycogen , biochemistry , glycogen synthase , nucleic acid sequence , enzyme , gene
A full‐length cDNA encoding the putative hepatic glycogen‐binding (G L ) 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 (G M ) subunit of PP1 from striated muscle. The similarities between G M and G L were most striking between residues 63–86, 144–166 and 186–227 of human G M (∼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 G L .