The primary structure of the precursor of chicken mitochondrial aspartate aminotransferase. Cloning and sequence analysis of cDNA

J Biol Chem. 1985 Dec 25;260(30):16060-3.


The mitochondrial isoenzyme of aspartate amino-transferase (mAspAT; subunit Mr 45,000) is synthesized on free polysomes in the cytosol as a precursor of higher Mr (pre-mAspAT; Sonderegger, P., Jaussi, R., Christen, P., and Gehring, H. (1982) J. Biol. Chem. 257, 3339-3345). We have isolated three overlapping cDNA clones that correspond almost to the full length of pre-mAspAT mRNA with 100 nucleotides at the 5' end missing. The mRNA is 2.1 kilobase pairs long and has a 3' noncoding region of 0.7 kilobase pairs. The cDNAs code for the 401 amino acid residues of mAspAT plus an NH2-terminal pre-piece. Deviations from the reported amino acid sequence were found at positions 154 and 202 where the cDNA specifies Gln instead of Glu. The pre-piece consists of 22 amino acid residues, among them 4 arginine and no acidic residues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aspartate Aminotransferases / genetics*
  • Base Composition
  • Base Sequence
  • Chickens
  • Cloning, Molecular*
  • DNA / metabolism*
  • Enzyme Precursors / genetics*
  • Isoenzymes / genetics
  • Liver / enzymology
  • Mitochondria, Liver / enzymology*
  • Molecular Weight
  • Polyribosomes / enzymology
  • RNA, Messenger / genetics
  • Templates, Genetic


  • Enzyme Precursors
  • Isoenzymes
  • RNA, Messenger
  • DNA
  • Aspartate Aminotransferases

Associated data

  • GENBANK/M12105