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

W. Zhang, M. F. Browner, R. J. Fletterick, A. A. DePaoli-Roach, P. J. Roach

Research output: Contribution to journalArticle

28 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)2532-2536
Number of pages5
JournalFASEB Journal
Volume3
Issue number13
DOIs
StatePublished - 1989

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Fingerprint Dive into the research topics of 'Primary structure of rabbit skeletal muscle glycogen synthase deduced from cDNA clones'. Together they form a unique fingerprint.

  • Cite this