hflB, a new Escherichia coli locus regulating lysogeny and the level of bacteriophage lambda cII protein.
The level of the viral cII protein has been proposed to be the crucial determinant in the lysis-lysogeny decision of bacteriophage lambda. A new Escherichia coli locus (hflB) has been identified in which a mutation (hflB29) leads to high frequency of lysogeny by lambda. A double mutant defective in both hflB and the previously identified hflA gene displays a more severe Hfl- phenotype than either single mutant. The hflB locus is at 69 minutes on the E. coli map, 85% co-transducible with argG. The hflB29 mutation results in increased stability of the phage cII protein (increasing its half-life twofold) and is recessive to hflB+. We conclude that the hflB+ locus is a negative regulator of cII, perhaps coding for or regulating a protease that acts on cII. In addition, we observe that the can1 mutation, an alteration of the cII gene that results in enhanced lysogenization, leads to increased stability of cII protein. These observations reinforce the view that the level of cII is a key factor in the lysis-lysogeny decision of lambda.
D010582:Bacteriophage lambda / Q000235:genetics*; D002874:Chromosome Mapping; D004926:Escherichia coli / Q000235:genetics*; D008242:Lysogeny; D009154:Mutation; D010641:Phenotype; D014764:Viral Proteins / Q000096:biosynthesis*
D014764:Viral Proteins