Bacteriophage-host interaction and restriction of nonglucosylated T6.
Nonglucosylated T6 phage (T6gtam 16am30, hereafter called T6alpha gt-) were found to have two structural anomalies when compared with wild-type T6. The DNA of T6alpha gt- phage contains single-strand interruptions. These can be seen both during infection, in the pool of replicating DNA, and in DNA extracted from purified phage. In addition, the sodium dodecyl sulfate-polyacrylamide gel pattern of T6alpha gt- phage structural proteins reveals a protein band not found in T6. The altered protein has a mobility slightly faster than that of the major head protein, and it is not removed by osmotic shock. The restriction activity of Escherichia coli B directed against T6alpha gt- phage is abolished by preinfection of the cells for 4 min with T4 im m2. The shut-off of restriction is observed either by the rescue of superinfecting T6alpha gt- or by the failure to detect degradation of incoming T6alpha gt- DNA. This effect is resistant to rifampin and chloramphenicol.
D002250:Carbon Radioisotopes; D002501:Centrifugation, Zonal; D002701:Chloramphenicol / Q000494:pharmacology; D003090:Coliphages / Q000032:analysis / Q000187:drug effects; D004267:DNA Viruses; D004269:DNA, Bacterial / Q000032:analysis; D004279:DNA, Viral / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D005827:Genetics, Microbial; D005947:Glucose; D007930:Leucine; D012293:Rifampin / Q000494:pharmacology; D014316:Tritium; D014764:Viral Proteins / Q000032:analysis
D002250:Carbon Radioisotopes; D004269:DNA, Bacterial; D004279:DNA, Viral; D014764:Viral Proteins; D014316:Tritium; D002701:Chloramphenicol; D007930:Leucine; D005947:Glucose; D012293:Rifampin