Lysogenization of Escherichia coli by bacteriophage Lambda: complementary activity of the host's DNA polymerase I and ligase and bacteriophage replication proteins Q and P.
When bacteriophage lambda DNA replication is blocked by mutation in phage genes O or P, the efficiency of lysogenization drops to a very low value unless high multiplicities of infecting phage are used. Our results show that even at high multiplicity, lambda O or P mutants cannot efficiently lysogenize some hosts that are defective in either DNA polymerase I or DNA ligase. Covalent closure of infecting DNA molecules, a preliminary step for insertion according to Campbell's model and an obvious candidate for this lysogenization defect, appears to occur normally under our conditions. In addition, prophage excision as measured by the frequency of curing O- and P- lysogens seemed normal when tested in the poll- strain. These results suggest that the Escherichia coli enzymes DNA polymerase I and ligase, and phage proteins O and P, are able to provide some complementary activity whose function is required specifically for prophage integration.
D003090:Coliphages / Q000254:growth & development / Q000378:metabolism*; D004254:DNA Nucleotidyltransferases / Q000096:biosynthesis*; D004261:DNA Replication; D004279:DNA, Viral / Q000096:biosynthesis*; D004926:Escherichia coli / Q000201:enzymology*; D005796:Genes; D008242:Lysogeny; D009154:Mutation; D011118:Polynucleotide Ligases / Q000096:biosynthesis*; D014779:Virus Replication
D004279:DNA, Viral; D004254:DNA Nucleotidyltransferases; D011118:Polynucleotide Ligases