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The bacterial phosphotransferase system (PTS) catalyzes the transfer of the phosphoryl group from phosphoenolpyruvate to its sugar substrates, PTS sugars, concomitant with the translocation of these sugars across the bacterial membrane. The phosphorylation of a given sugar requires four proteins, two general proteins, Enzyme I, and the histidine-containing phosphocarrier protein of the PTS (HPr), used for all sugars, and a pair of proteins specific for that sugar, designated an Enzyme II complex. The phosphotransferase system has been implicated in regulating the induction of synthesis of some catabolic enzyme systems required for the utilization of sugars that are not substrates of the phosphotransferase system, and this and the accompanying reports are concerned with this phenomenon in Salmonell typhimurium and Escherichia coli. Mutants defective in Enzyme I (ptsI), HPr (ptsH), and certain Enzymes II were isolated, and their abilities to ferment and grow on a wide range of sugars and other compounds were determined. The mutants showed the expected properties on PTS sugars, but in addition, ptsH and tight ptsI mutants were unable to utilize certain non-PTS sugars, including maltose, melibiose, glycerol, glycerol-P, mannose-6-P, and, in E. coli, lactose. Leaky Enzyme I mutants could utilize these carbohydrates, but were unable to use them in the presence of a PTS sugar such as methyl alpha-D-glucopyranoside. In accord with the results reported by other laboratories, the inability of the mutants to utilize the non-PTS sugars was explained by the fact that these cells could not be normally induced to synthesize the corresponding catabolic enzyme systmes. This phenomenon is designated PTS-mediated repression. PTS-mediated repression was also observed in wild type cells, but by comparing wild type and leaky pts mutants it was shown that the sensitivity to repression by PTS sugars was greatest in mutants containing the lowest levels of Enzyme I or HPr. Furthermore, ptsI mutants containing a second site mutation in a gene for an Enzyme II were not repressed by the sugar substrate of that Enzyme II, although repression by other PTS sugars was not affected. Transport and other studies further indicated that neither appreciable uptake nor metabolism of the PTS sugars was required for these compounds to effect repression. The ptsH mutants showed the same phenotypic properties as the ptsI mutants with some important exceptions. First, they could ferment and grow on a PTS sugar, fructose. Second, after growth on fructose, (and to a lesser extent on glucose or mannose), such mutants were capable of utilizing other PTS sugars for a few generations. Third, growth of the ptsH mutants on fructose relieved PTS-mediated repression; after growth on fructose, but not on lactate, the mutants could grow for several generations on non-PTS sugars. Preliminary experiments indicated that growth on fructose resulted in the formation of one or more proteins that could substitute for HPr in the utilization of both PTS and non-PTS sugars.
Simoni et al. (Mon,) studied this question.