Yeast carbamyl phosphate synthetase. Structure of the yeast gene and homology to Escherichia coli carbamyl phosphate synthetase.

C. J. Lusty, E. E. Widgren, K. E. Broglie, Hiroshi Nyunoya

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Abstract

A cloned fragment of yeast chromosomal DNA carrying the gene CPA2 coding for the large subunit of arginine-specific carbamyl phosphate synthetase has been sequenced. The cloned DNA has a 3,354-nucleotide long continuous reading frame coding for a polypeptide of 1,117 amino acids. The calculated molecular weight of the encoded polypeptide is 123,787, in good agreement with the reported molecular weight of the yeast carbamyl phosphate synthetase large subunit. The amino acid sequence of yeast carbamyl phosphate synthetase is homologous to the recently determined sequence of Escherichia coli carbamyl phosphate synthetase (Nyunoya, H., and Lusty, C. J. (1983) Proc. Natl. Acad. Sci. U. S. A. 80, 4629-4633) over almost the entire length of the protein. Like the E. coli large subunit, the yeast enzyme exhibits an extensive internal homology between its NH2- and carboxyl-terminal halves. The internal homology in both the yeast and E. coli proteins indicates that the gene coding for the large subunit of carbamyl phosphate synthetase was derived from a tandem duplication which occurred prior to the divergence of eukaryotes and prokaryotes.

Original languageEnglish
Pages (from-to)14466-14477
Number of pages12
JournalJournal of Biological Chemistry
Volume258
Issue number23
Publication statusPublished - 1983 Dec 10
Externally publishedYes

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Carbamyl Phosphate
Ligases
Yeast
Escherichia coli
Genes
Yeasts
Molecular Weight
Molecular weight
Amino Acids
Reading Frames
Peptides
Escherichia coli Proteins
DNA
Eukaryota
Arginine
Amino Acid Sequence
Nucleotides
Enzymes
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Yeast carbamyl phosphate synthetase. Structure of the yeast gene and homology to Escherichia coli carbamyl phosphate synthetase. / Lusty, C. J.; Widgren, E. E.; Broglie, K. E.; Nyunoya, Hiroshi.

In: Journal of Biological Chemistry, Vol. 258, No. 23, 10.12.1983, p. 14466-14477.

Research output: Contribution to journalArticle

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