Identification and mutational analysis of bacteriophage PRD1 holin protein P35

J Bacteriol. 2003 Jul;185(13):3795-803. doi: 10.1128/JB.185.13.3795-3803.2003.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Bacteriolysis
  • Bacteriophage PRD1 / genetics*
  • Bacteriophage PRD1 / metabolism
  • Bacteriophage PRD1 / physiology
  • Base Sequence
  • Cloning, Molecular
  • DNA Mutational Analysis
  • Escherichia coli / physiology
  • Escherichia coli / virology
  • Lipoproteins
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Mutation*
  • N-Acetylmuramoyl-L-alanine Amidase
  • Salmonella typhimurium / physiology
  • Salmonella typhimurium / virology
  • Viral Proteins / chemistry
  • Viral Proteins / genetics*
  • Viral Proteins / metabolism


  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Lipoproteins
  • Membrane Proteins
  • P35 protein, Enterobacteria phage PRD1
  • Viral Proteins
  • LytH protein, Staphylococcus aureus
  • N-Acetylmuramoyl-L-alanine Amidase