Using a mini-Tn5lacZ1 reporter transposon, lacZ fusions have been identified in Proteus mirabilis that are activated by the accumulation of self-produced extracellular signals. Genes identified by this approach include putative homologs of pgm, nlpA and two genes of unknown function. The extracellular signal(s) involved in activation were resistant to the effects of acid and alkali. The signal required for activation of (nlpA) cma482::lacZ was sensitive to protease, suggesting the signal is a peptide or small protein. The signals behaved as polar molecules and were not extractable with ethyl acetate. A mini-Tn5Cm insertion was identified in a probable ptsI homolog that blocked activation of the cma134::lacZ fusion by an extracellular signal. The ptsI mutation did not alter extracellular signal production and may have a role in signal response. © 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
Sturgill, G. M., Siddiqui, S., Ding, X., Pecora, N. D., & Rather, P. N. (2002). Isolation of lacZ fusions to Proteus mirabilis genes regulated by intercellular signaling: Potential role for the sugar phosphotransferase (Pts) system in regulation. FEMS Microbiology Letters, 217(1), 43–50. https://doi.org/10.1016/S0378-1097(02)01043-1