Abstract
Maximum lysogenization of E. coli by bacteriophage lambda requires both the lambdacIII gene function and the host catabolite gene activation system mediated by adenosine 3':5'-cyclic monophosphate. Whereas considerable lysogenization occurs in the presence of either system alone, lysogenization is absolutely prevented in the absence of both systems. Neither system is, however, required for efficient lysogenization when the host bears an hfl(-) mutation. It is argued that the normal function of these two systems is to negate the antagonistic effect of the Hfl(+) protein upon lysogenization. It is further argued that both the lambdacIII gene function and the Hfl(+) protein do not directly affect the host catabolite gene activation system.
MeSH Terms
Adenylyl Cyclases/biosynthesis
Coliphages/metabolism
Cyclic AMP/metabolism
DNA Viruses/metabolism
Escherichia coli/enzymology,metabolism
Galactose/metabolism
Genes
Genes, Regulator
Genotype
Lactose/metabolism
Lysogeny
Malates/metabolism
Mutation
Operon
Phenotype
Transcription, Genetic
Transduction, Genetic
Chemicals
Malates
Cyclic AMP
Adenylyl Cyclases
Lactose
Galactose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Belfort M
Wulff D
References (12)
12 references, click to expand
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