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The ltp gene, located within the lysogeny module of temperate Streptococcus thermophilus phage TP-J34, has been shown to be expressed in lysogenic strain S. thermophilus J34. It codes for a lipoprotein, as demonstrated by inhibition of cleavage of the signal sequence by globomycin. Exposure of Ltp on the surface of Lactococcus lactis protoplasts bearing a plasmid-encoded copy of ltp has been demonstrated...
The temperate Streptococcus thermophilus bacteriophage TP-J34 was identified in the lysogenic host strain J34. The majority of phage particles produced upon induction was defective and noninfectious, consisting of DNA-filled heads lacking tails. A physical map (45.6 kb) was established. Analysis of minor restriction bands of the DNA isolated from phage particles as well as the analysis of the protein...
A 7.6-kb DNA segment covering the putative lysogeny module of thepac-site-containing temperateStreptococcus thermophilusbacteriophage TP-J34 was sequenced. Sequence alignment with the lysogeny module from thecos-site-containingS. thermophilusbacteriophage φSfi21 revealed areas of high sequence conservation (e.g., over theintgene), interspersed with regions of low or no sequence similarity (e.g., over...
The receptor-binding protein pb5 T5 of bacteriophage T5, when expressed from theoadgene cloned in pVK88 under the control of the phage T7 promoter/polymerase system, has been shown to bind to its FhuA receptor on the surface ofE. coli,where it blocks FhuA for subsequent adsorption of T5 (Mondigleret al., FEMS Microbiol. Lett.,130, 293–300, 1995). In the present study the blocking assay has...
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