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Nucleic Acids Research, 1984, Vol. 12, No. 24 9427-9440
© 1984

MOLECULAR BIOLOGY

The complete nucleotide sequence of the adenylate cyclase gene of Escherichia coli

Hiroji Aiba1,*, Kazuyasu Mori1, Minoru Tanaka1, Tatsuo Ooi2, Anne Roy3 and Antoine Danchin3

1Radioisotope Lab., Faculty of Medicine, Kyoto Univ. Kyoto 606 2Dept. Enzyme Chemistry, Inst. Chemical Research, Kyoto Univ. Uji, Kyoto 611, Japan 3Dépt. Biochimie et Génétique Moléculaire, Inst.Pasteur 28 rue du Docteur Roux, 75724, Paris Cédex 15, France

*To whom reprint requests should be sent

Received November 19, 1984. Accepted November 23, 1984.

The complete nucleotide sequence of the cya gene from E. coli was determined. The gene encodes a polypeptide consisting of 848 amino acid residues with a calculated molecular weight of 97,542. The deduced protein structure reveals that cyclase is comprised of two domains, an amino-terminal region exhibiting catalytic activity and a carboxy-terxninal region possibly carrying regulatory function. The frequent appearance of rare codons in the beginning of the gene as well as the sequence duplication in the promoter-initiator region suggest possible regulation(s) at the translational level. An unknown gene (cyaX) which seems to code for a very hydrophobic protein was found following the cya gene. Sequence analysis suggests that the cyaX is a part of the cya operon.


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