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Nucleic Acids Research, 1985, Vol. 13, No. 3 943-952
© 1985

Articles

A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites

Jan P. Kraus, Peter E. Hodges, Cynthia L. Williamson, Arthur L. Horwich, Frantisek Kalousek, Kenneth R. Williams* and Leon E. Rosenberg

Departments of Human Genetics, Yale University School of Medicine New Haven, CT 06510, USA *Departments of Molecular Biophysics and Biochemistry, Yale University School of Medicine New Haven, CT 06510, USA

Received December 6, 1984. Accepted January 6, 1985.

We have cloned a DNA complementary to the messenger RNA encoding the precursor of ornithine transcarbamylase from rat liver. This complementary DNA contains the entire protein coding region of 1062 nucleotides and 86 nucleotides of 5'- and 298 nucleotides of 3'-untranslated sequences. The predicted amino acid sequence has been confirmed by extensive protein sequence data. The mature rat enzyme contains the same number of amino acid residues (322) as the human enzyme and their amino acid sequences are 93% homologous. The rat and human amino-terminal leader sequences of 32 amino acids, on the other hand, are only 69% homoloceus. The rat leader contains no acidic and seven basic residues compared to four basic residues found in the human leader. There is complete sequence homology (residues 58–62) among the ornithine and aspartate transcerbamylases from E.coli and the rat and human ornithine transcarbamylases at the carbamyl phosphate binding site. Finally, a cysteine containing hexapeptide (residues 268–273), the putative ornithine binding site in Streptococcus faecalis, Streptococcus faecium, and bovine transcarbamylases, is completely conserved among the two E.coli and the two mammalian transcarbamylases.


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