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Nucleic Acids Research, 1983, Vol. 11, No. 8 2465-2477
© 1983

MOLECULAR BIOLOGY

Molecular structure and function of the bacteriocin gene and bacteriocin protein of plasmid Clo DF13

Peter J.M. van den Elzen, Hanneke H.B. Walters, Eduard Veltkamp and H.John J. Nijkamp

Department of Genetics, Biological Laboratory, Vrije Universiteit De Boelelaan 1087, 1981 HV Amsterdam, The Netherlands

Received January 4, 1983. Revised March 2, 1983. Accepted March 2, 1983.

In this paper we present the complete nucleotide sequence of the bacteriocin gene of plasmid Clo DF13. According to the predicted aminoacid sequence the bacteriocin, cloacin DF13, consists of 561 aminoacids and has a molecular weight of 59,293 D. To obtain insight into the structure and function of specific parts of the cloacin molecule, we constructed a hydration profile and we predicted the secondary structure of the protein. According to our predictions, the N-terminus of cloacin DF13 (corresponding to the first 150–180 aminoacids) is relatively hydrophobic and is rich in glycine residues. The data obtained support previous findings that the N-terminal part of cloacin DF13 is involved in translocation of this protein across the cell membrane. The C-terminal part of the cloacin protein is rich in positively charged aminoacids; this might reflect the RNase activity located within this domain. A comparison of the bacteriocin genes and corresponding proteins of Clo DF13 and Col El did not reveal any homology at the level of either the nucleotide or the aminoacid sequence. The codon usage of both genes, however, exhibits striking similarities. The sequence data obtained during this study enabled us to present the nucleotide sequence of the entire cloacin operon. The structure of this operon and the regulation of expression of the genes, located within this operon, is discussed.


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