The hydrophilic C-terminal part of the lambda S holin is non-essential for intermolecular interactions.
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.
Rietsch
A
A
Institute of Microbiology and Genetics, Vienna Biocenter, University of Vienna, Austria.
Fraisl
P
P
Graschopf
A
A
Bläsi
U
U
D000595:Amino Acid Sequence; D001433:Bacteriolysis / Q000502:physiology*; D010582:Bacteriophage lambda / Q000737:chemistry* / Q000235:genetics; D002462:Cell Membrane / Q000737:chemistry; D004926:Escherichia coli / Q000821:virology*; D008969:Molecular Sequence Data; D009154:Mutation; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics
C029555:E protein, bacteriophage X174; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins; C082001:bacteriophage lambda lysis effector protein S105; C082002:bacteriophage lambda lysis inhibitor protein S107