Volume 6, Issue 10 pp. 1335-1344
Full Access

Characterization of the Escherichia coli codBA operon encoding cytosine permease and cytosine deaminase

S. Danielsen

S. Danielsen

Institute of Biological Chemistry B, University of Copenhagen, Solvgade 83. DK-1307 Copenhagen K, Denmark.

Search for more papers by this author
M. Kilstrup

Corresponding Author

M. Kilstrup

Institute of Biological Chemistry B, University of Copenhagen, Solvgade 83. DK-1307 Copenhagen K, Denmark.

*For correspondence. Tel. (33) 116062; Fax (33) 145058.Search for more papers by this author
K. Barilla

K. Barilla

Institute of Biological Chemistry B, University of Copenhagen, Solvgade 83. DK-1307 Copenhagen K, Denmark.

Department of Chemistry, University of Regina, Regina, Saskatchewan, Canada S4S 0A2.

Search for more papers by this author
B. Jochimsen

B. Jochimsen

Department of Molecular Biology, University of Aarhus, DK-8000 Arhus C., Denmark.

Search for more papers by this author
J. Neuhard

J. Neuhard

Institute of Biological Chemistry B, University of Copenhagen, Solvgade 83. DK-1307 Copenhagen K, Denmark.

Search for more papers by this author
First published: May 1992
Citations: 105

Summary

The nucleotide sequence of a 3.1 kb segment carrying the cytosjne deaminase gene (codA) from Esctierichia coli was determined. The sequence revealed the presence of two open reading frames, the first (codB) specifying a highly hydrophobic polypeptide and the second specifying cytosine deaminase. A two-codon overlap between the two reading frames indicates that they constitute an operon. Transcription of the operon was found to be regulated by exogenous purines. Polypeptides specified by each of the two reading frames were expressed in minicells, and the codB gene product was found to be highly enriched in the membrane fraction. Uptake experiments showed that the CodB protein is required for cytosine transport into the cell and that the intracellular accumulation of cytosine correlated with the codB gene dose. A topological model for the cytosine permease in the cytoplasmic membrane is proposed.

The full text of this article hosted at iucr.org is unavailable due to technical difficulties.