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Journal of Bacteriology, March 2005, p. 2050-2057, Vol. 187, No. 6
0021-9193/05/$08.00+0     doi:10.1128/JB.187.6.2050-2057.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Nucleotide Sequence of the Head Assembly Gene Cluster of Bacteriophage L and Decoration Protein Characterization

Eddie B. Gilcrease,¹ Danella A. Winn-Stapley,^1, F. Curtis Hewitt,¹ Lisa Joss,² and Sherwood R. Casjens^1*

Division of Cell Biology and Immunology, Department of Pathology,¹ Department of Biochemistry, University of Utah Medical School, Salt Lake City, Utah²

Received 28 October 2004/ Accepted 8 December 2004

The temperate Salmonella enterica bacteriophage L is a close relative of the very well studied bacteriophage P22. In this study we show that the L procapsid assembly and DNA packaging genes, which encode terminase, portal, scaffold, and coat proteins, are extremely close relatives of the homologous P22 genes (96.3 to 99.1% identity in encoded amino acid sequence). However, we also identify an L gene, dec, which is not present in the P22 genome and which encodes a protein (Dec) that is present on the surface of L virions in about 150 to 180 molecules/virion. We also show that the Dec protein is a trimer in solution and that it binds to P22 virions in numbers similar to those for L virions. Its binding dramatically stabilizes P22 virions against disruption by a magnesium ion chelating agent. Dec protein binds to P22 coat protein shells that have expanded naturally in vivo or by sodium dodecyl sulfate treatment in vitro but does not bind to unexpanded procapsid shells. Finally, analysis of phage L restriction site locations and a number of patches of nucleotide sequence suggest that phages ST64T and L are extremely close relatives, perhaps the two closest relatives that have been independently isolated to date among the lambdoid phages.

Present address: Biology Department, MIT, Cambridge, MA 02139.

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