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Journal of Bacteriology, October 1999, p. 6463-6468, Vol. 181, No. 20
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Identification and Characterization of the Single-Stranded DNA-Binding Protein of Bacteriophage P1

Hansjörg Lehnherr,* Jannick D. Bendtsen, Fabian Preuss, and Tatiana V. Ilyina

Institute of Molecular Biology, University of Southern Denmark, Main Campus Odense University, DK-5230 Odense M, Denmark

Received 19 April 1999/Accepted 6 July 1999

The genome of bacteriophage P1 harbors a gene coding for a 162-amino-acid protein which shows 66% amino acid sequence identity to the Escherichia coli single-stranded DNA-binding protein (SSB). The expression of the P1 gene is tightly regulated by P1 immunity proteins. It is completely repressed during lysogenic growth and only weakly expressed during lytic growth, as assayed by an ssb-P1/lacZ fusion construct. When cloned on an intermediate-copy-number plasmid, the P1 gene is able to suppress the temperature-sensitive defect of an E. coli ssb mutant, indicating that the two proteins are functionally interchangeable. Many bacteriophages and conjugative plasmids do not rely on the SSB protein provided by their host organism but code for their own SSB proteins. However, the close relationship between SSB-P1 and the SSB protein of the P1 host, E. coli, raises questions about the functional significance of the phage protein.

* Corresponding author. Mailing address: Institute of Molecular Biology, University of Southern Denmark, Main Campus Odense University, Campusvej 55, DK-5230 Odense M, Denmark. Phone: 65 50 23 74. Fax: 65 93 27 81. E-mail: lehnherr{at}biobase.dk.

Journal of Bacteriology, October 1999, p. 6463-6468, Vol. 181, No. 20
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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