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Primary structure of rabbit skeletal muscle glycogen synthase deduced from cDNA clones
Author(s) -
Zhang Weiming,
Browner Michelle F.,
Fletterick Robert J.,
DepaoliRoach Anna A.,
Roach Peter J.
Publication year - 1989
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.3.13.2509275
Subject(s) - complementary dna , skeletal muscle , microbiology and biotechnology , untranslated region , messenger rna , protein primary structure , biology , peptide sequence , nucleic acid sequence , glycogen synthase , biochemistry , coding region , amino acid , gene , glycogen , anatomy
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 NH 2 ‐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 NH 2 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.—Z hang , W.; B rowner , M. F.; F letterick , R. J.; D e P aoli ‐R oach , A. A.; R oach , P.J. Primary structure of rabbit skeletal muscle glycogen synthase deduced from cDNA clones. FASEB J. 3: 2532‐2536; 1989.