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

FEBS Letters

Moorhead, Greg¹  Morrice, Nick¹  Cohen, Patricia T.W.¹  Doherty, Martin J.¹  Cohen, Philip¹ 

[1] Medical Research Council Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland, UK

关键词: Protein phosphatase;    Targetting subunit;    Glycogen;    Glycogen metabolism;    Cyclic AMP-dependent protein kinase;   

DOI  :  10.1016/0014-5793(95)01184-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown