Bacteriophage PRD1 DNA entry uses a viral membrane-associated transglycosylase activity.
Amino acid sequence analyses have indicated that the amino-terminal part of bacteriophage PRD1 structural protein P7 carries a conserved transglycosylase domain. We analysed wild-type PRD1 and different mutant particles in zymograms and found a glycolytic activity that was associated with protein P7. This is the first time a putative bacteriophage or plasmid lytic transglycosylase has been shown to have an enzymatic activity. In the absence of protein P7, the phage DNA replication and host cell lysis were delayed. Gene VII of PRD1 is known to encode proteins P7 and P14. In this investigation, the open reading frame coding for P14 was mapped to the 3' end of gene VII. Proteins P7 and P14 probably form a heteromultimeric complex, which is located at the particle vertices and is involved in the early steps of the PRD1 life cycle
Rydman
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Department of Biosciences and Institute of Biotechnology, Viikki Biocenter, University of Helsinki, PO Box 56 (Viikinkaari 5), FIN-00014, Finland.
Bamford
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DH
D002462:Cell Membrane; D004261:DNA Replication; D004279:DNA, Viral / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D016695:Glycosyltransferases / Q000235:genetics / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism; D017434:Protein Structure, Tertiary; D017916:Tectiviridae / Q000201:enzymology* / Q000502:physiology; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D014779:Virus Replication
D004279:DNA, Viral; D010457:Peptidoglycan; D014764:Viral Proteins; D016695:Glycosyltransferases