AMINO-ACID-SEQUENCE AND EXPRESSION OF THE HEPATIC GLYCOGEN-BINDING (G(L))-SUBUNIT OF PROTEIN PHOSPHATASE-1

被引:132
作者
DOHERTY, MJ [1 ]
MOORHEAD, G [1 ]
MORRICE, N [1 ]
COHEN, P [1 ]
COHEN, PTW [1 ]
机构
[1] UNIV DUNDEE, DEPT BIOCHEM, MRC, PROT PHOSPHORYLAT LAB, DUNDEE DD1 4HN, SCOTLAND
来源
FEBS LETTERS | 1995年 / 375卷 / 03期
基金
英国医学研究理事会; 加拿大自然科学与工程研究理事会;
关键词
PROTEIN PHOSPHATASE; TARGETING SUBUNIT; GLYCOGEN; GLYCOGEN METABOLISM; CYCLIC AMP-DEPENDENT PROTEIN KINASE;
D O I
10.1016/0014-5793(95)01184-G
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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) (similar to 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).
引用
收藏
页码:294 / 298
页数:5
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