Cell Growth and λ Phage Development Controlled by the Same Essential Escherichia coli Gene, ftsH/hflB

• Published in: Proceedings of the National Academy of Sciences - PNAS 1993-11, Vol.90 (22), p.10861-10865
• Main Authors: Herman, Christophe, Ogura, Teru, Tomoyasu, Toshifumi, Hiraga, Sota, Akiyama, Yoshinori, Ito, Koreaki, Thomas, Rene, D'Ari, Richard, Bouloc, Philippe
• Format: Article
• Language: English
• Subjects: Adenosine triphosphatases; ATP-Dependent Proteases; Bacterial Proteins - metabolism; Bacterial Proteins - physiology; Bacteriophage lambda - growth & development; Bacteriophages; Biological and medical sciences; Cell Division; Cell growth; Cloning, Molecular; Endopeptidases - physiology; Escherichia coli; Escherichia coli - growth & development; Escherichia coli Proteins; Fundamental and applied biological sciences. Psychology; Gene expression regulation; Gene Expression Regulation, Bacterial; Genes; Genes, Bacterial; Genetic mutation; Infections; Lysogeny; Membrane Proteins - metabolism; Microbiology; Phenotype; Phenotypes; Plasmids; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; Repressor Proteins - physiology; Transcription Factors - metabolism; Viral Proteins; Virology
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.90.22.10861

The λ phage choice between lysis and lysogeny is influenced by certain host functions in Escherichia coli. We found that the frequency of λ lysogenization is markedly increased in the ftsH1 temperature-sensitive mutant. The ftsH gene, previously shown to code for an essential inner membrane protein with putative ATPase activity, is identical to hflB, a gene involved in the stability of the phage cII activator protein. The lysogenic decision controlled by FtsH/HflB is independent of that controlled by the protease HflA. Overproduction of FtsH/HflB suppresses the high frequency of lysogenization in an hflA null mutant. The FtsH/HflB protein, which stimulates cII degradation, may be a component of an HflA-independent proteolytic pathway, or it may act as a chaperone, maintaining cII in a conformation subject to proteolysis via such a pathway. Suppressor mutations of ftsH1 temperature-sensitive lethality, located in the fur gene (coding for the ferric uptake regulator), did not restore FtsH/HflB activity with respect to λ lysogenization.