par Herman, Christophe ;D'Ari, Richard;Bouloc, Philippe;Ogura, Teru;Tomoyasu, Toshifumi;Hiraga, Sota;Akiyama, Yoshinori;Ito, Koreaki;Thomas, René
Référence Proceedings of the National Academy of Sciences of the United States of America, 90, 22, page (10861-10865)
Publication Publié, 1993-11
Référence Proceedings of the National Academy of Sciences of the United States of America, 90, 22, page (10861-10865)
Publication Publié, 1993-11
Article révisé par les pairs
Résumé : | 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. |