PMID: 2509275Nov 1, 1989Paper

Primary structure of rabbit skeletal muscle glycogen synthase deduced from cDNA clones

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
W M ZhangP J Roach

Abstract

The complete amino acid sequence of rabbit skeletal muscle glycogen synthase was deduced from cDNA clones with a composite length of 3317 bp. An mRNA of 3.6 kb was identified by Northern blot analysis of rabbit skeletal muscle RNA. The mRNA coded for a protein of 734 residues with a molecular weight of 83,480. The deduced NH2-terminal and COOH-terminal sequences corresponded to those reported for the purified protein, indicating the absence of any proteolytic processing. At the nucleotide level, the 5' untranslated and coding regions were 79 and 90% identical for rabbit and human muscle glycogen synthases, whereas the 3' untranslated regions were significantly less similar. The enzymes had 97% amino acid sequence identity. Interestingly, the NH2 and COOH termini of rabbit and human muscle glycogen synthase, the regions of phosphorylation, showed the greatest sequence variation (15 of 19 mismatches and two insertion/deletion events), which may indicate different evolutionary constraints in the regulatory and catalytic regions of the molecule.

Citations

Aug 5, 2000·The Journal of Biological Chemistry·E CidJ C Ferrer
May 26, 1995·The Journal of Biological Chemistry·A V Skurat, P J Roach
Sep 26, 2002·FEBS Letters·Emili CidJuan C Ferrer
Jun 1, 1995·The International Journal of Biochemistry & Cell Biology·D GrekinisK K Schlender
Jun 1, 1996·Brain Research. Molecular Brain Research·G PellegriJ L Martin
Dec 1, 1996·The Journal of Steroid Biochemistry and Molecular Biology·X SuS Shapiro
Oct 24, 2006·Archives of Biochemistry and Biophysics·Alexander V SkuratPeter J Roach
Jan 1, 1991·Advances in Enzyme Regulation·P J RoachT W Hrubey

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