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Journal of Bacteriology, July 2003, p. 3795-3803, Vol. 185, No. 13
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.13.3795-3803.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Identification and Mutational Analysis of Bacteriophage PRD1 Holin Protein P35

Pia S. Rydman and Dennis H. Bamford^*

Department of Biosciences and Institute of Biotechnology, Viikki Biocenter, University of Helsinki, Finland

Received 22 January 2003/ Accepted 5 April 2003

Holin proteins are phage-induced integral membrane proteins which regulate the access of lytic enzymes to host cell peptidoglycan at the time of release of progeny viruses by host cell lysis. We describe the identification of the membrane-containing phage PRD1 holin gene (gene XXXV). The PRD1 holin protein (P35, 12.8 kDa) acts similarly to its functional counterpart from phage lambda (gene S), and the defect in PRD1 gene XXXV can be corrected by the presence of gene S of lambda. Several nonsense, missense, and insertion mutations in PRD1 gene XXXV were analyzed. These studies support the overall conclusion that the charged amino acids at the protein C terminus are involved in the timing of host cell lysis.

Present address: Geneos Ltd., FIN-00251 Helsinki, Finland.

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