The hydrophilic C-terminal part of the lambda S holin is non-essential for intermolecular interactions

FEMS Microbiol Lett. 1997 Aug 15;153(2):393-8. doi: 10.1111/j.1574-6968.1997.tb12601.x.


Available evidence indicates that oligomerization of the bacteriophage lambda S holin leads to a non-specific lesion in the cytoplasmic membrane which permits transit of the phage encoded transglycosylase to the periplasm. In an attempt to locate an intermolecular interaction domain in S a chimeric protein comprising the N-terminal 32 aa of phage PhiX174 lysis protein E and the last 75 aa of lambda S has been constructed. We report that the E phi S fusion protein is stable, membrane bound, and inhibits S-mediated lysis in trans. C-terminal truncations of the E phi S fusion protein indicated that the hydrophilic C-terminal end of S (i.e. the last 15 aa) is non-essential for oligomerization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacteriolysis / physiology*
  • Bacteriophage lambda / chemistry*
  • Bacteriophage lambda / genetics
  • Cell Membrane / chemistry
  • Escherichia coli / virology*
  • Molecular Sequence Data
  • Mutation
  • Recombinant Fusion Proteins
  • Viral Proteins / chemistry*
  • Viral Proteins / genetics


  • E protein, bacteriophage X174
  • Recombinant Fusion Proteins
  • Viral Proteins
  • bacteriophage lambda lysis effector protein S105
  • bacteriophage lambda lysis inhibitor protein S107