Regulation of genes coding for enzyme constituents of the bacterial phosphotransferase system

@article{Rephaeli1980RegulationOG,
  title={Regulation of genes coding for enzyme constituents of the bacterial phosphotransferase system},
  author={Ada Rephaeli and Milton H. Saier},
  journal={Journal of Bacteriology},
  year={1980},
  volume={141},
  pages={658 - 663}
}
Regulation of the synthesis of the proteins of the phosphoenolpyruvate:sugar phosphotransferase system was systematically studied in wild-type and mutant strains of Salmonella typhimurium and Escherichia coli. The results suggest that enzyme I and HPr as well as the glucose-specific and the mannose-specific enzymes II are synthesized by a mechanism which depends on (i) cyclic adenosine monophosphate and its receptor protein; (ii) extracellular inducer; (iii) the sugar-specific enzyme II complex… Expand
Catalytic activities associated with the enzymes II of the bacterial phosphotransferase system.
  • M. Saier
  • Biology, Medicine
  • Journal of supramolecular structure
  • 1980
TLDR
Preliminary experiments suggest that the different functions of the Enzyme IImtl can be dissected by genetic and biochemical techniques, and emphasize the functional complexity of the PTS and its integral membrane protein constituents. Expand
Control of glucose metabolism by enzyme IIGlc of the phosphoenolpyruvate-dependent phosphotransferase system in Escherichia coli
TLDR
The quantitative effects of variations in the amount of enzyme IIGlc of the phosphoenolpyruvate:glucose phosphotransferase system (PTS) on glucose metabolism in Escherichia coli were studied and the implications for PTS-mediated regulation, i.e., inhibition of growth on non-PTS compounds by glucose, are discussed. Expand
YeeI, a Novel Protein Involved in Modulation of the Activity of the Glucose-Phosphotransferase System in Escherichia coli K-12
TLDR
By measuring the surface plasmon resonance, it is found that YeeI (proposed gene designation, mtfA) directly interacts with Mlc with high affinity, implying that the two proteins belong to the same signal transduction pathway and that Mlc is epistatic to Yeei. Expand
Enzyme I(Ntr) from Escherichia coli. A novel enzyme of the phosphoenolpyruvate-dependent phosphotransferase system exhibiting strict specificity for its phosphoryl acceptor, NPr.
TLDR
This is the first report demonstrating specificity at the level of the energy coupling proteins of the PTS, and suggests that E. coli possesses at least two distinct PTS phosphoryl transfer chains, EI(Ntr) --> NPr --> IIA(ntr) and EI --> HPr -->IIA(sugar). Expand
Negative regulation of the pts operon by Mlc: mechanism underlying glucose induction in Escherichia coli
The pts operon of Escherichia coli consists of three genes ptsH, ptsI and crr, each encoding for central components of the phosphoenolpyruvate: carbohydrate phosphotransferase system, HPr, enzyme IExpand
The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS): an interface between energy and signal transduction
  • B. Erni
  • Chemistry
  • Journal of the Iranian Chemical Society
  • 2012
The bacterial phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS) mediates the uptake and phosphorylation of carbohydrates, and is involved in signal transduction. It comprises twoExpand
Evidence for the evolutionary relatedness of the proteins of the bacterial phosphoenolpyruvate:Sugar phosphotransferase system
TLDR
Evidence is presented which suggests that these proteins share a common evolutionary origin and that a fructose‐specific phosphotransferase may have been the primordial ancestor of them all. Expand
Soluble sugar permeases of the phosphotransferase system in Escherichia coli: evidence for two physically distinct forms of the proteins in vivo
TLDR
It is proposed that enzymes II of the PTS exist in two physically distinct forms in the E. coli cell, one tightly integrated into the membrane and one either soluble or loosely associated with the membrane, and that the membrane‐integrated enzymes II are largely dimeric, whereas the soluble enzymes II, retarded during passage through a gel filtration column, are largely monomeric. Expand
Isolation of IIIGlc of the phosphoenolpyruvate-dependent glucose phosphotransferase system of Salmonella typhimurium
TLDR
A procedure for the isolation of IIIglc of Salmonella typhimurium, a protein component of the phosphoenolpyruvate-dependent sugar phosphotransferase system, and its affinity for octyl-Sepharose may be an indication of the partial hydrophobic nature of IIIGlc. Expand
Glucose Transporter Mutants of Escherichia coli K-12 with Changes in Substrate Recognition of IICBGlc and Induction Behavior of theptsG Gene
TLDR
A new regulatory mechanism involved in ptsG induction is postulated, which modulates IIC(Glc) which controls the repressor DgsA and hence ptsG expression and, by the same mechanism, glucose uptake and phosphorylation also control the expression of the pts operon and probably of all operons controlled by the represses. Expand
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TLDR
Transport and other studies further indicated that neither appreciable uptake nor metabolism of the PTS sugars was required for these compounds to effect repression, and this and the accompanying reports are concerned with this phenomenon in Salmonell typhimurium and Escherichia coli. Expand
Coordinate regulation of adenylate cyclase and carbohydrate permeases by the phosphoenolpyruvate:sugar phosphotransferase system in Salmonella typhimurium.
TLDR
It is suggested that the activities of adenylate cyclase and the permease proteins are subject to allosteric regulation and that the allosterics effector is a regulatory protein which can be phosphorylated by the phosphotransferase system. Expand
Sugar transport. The crr mutation: its effect on repression of enzyme synthesis.
TLDR
Assay of the PTS proteins in crr mutants showed that the only component detectably affected was a sugar-specific protein of theTS, Factor IIIG1c, involved in the phsophorylation of glucose (and methyl alpha-glucoside), and the crr gene appears to code for or regulate the synthesis of this protein. Expand
Sugar transport. II. Characterization of constitutive membrane-bound enzymes II of the Escherichia coli phosphotransferase system.
TLDR
It was shown that II-B, phosphatidylglycerol, and divalent cation interacted to give a sedimentable pellet which catalyzed the phosphorylation of the sugars in the presence of II-A and the phospho-HPr generating system. Expand
Isolation and Mapping of Phosphotransferase Mutants in Escherichia coli
Mutants of Escherichia coli K-12 defective in enzyme I or Hpr, the two common components of the phosphoenolpyruvate-dependent phosphotransferase system, were isolated by a simple, direct method. TheExpand
Phosphotransferase-system enzymes as chemoreceptors for certain sugars in Escherichia coli chemotaxis.
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TLDR
It was found that the transport specificity of a given enzyme II correlates with taxis specificity, and mutational loss of an enzyme II abolishes taxis toward only those sugars which it alone transports. Expand
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TLDR
Isolation of different proteins of the phosphotransferase system and reconstitution of the complex shows that in the net transfer of the phosphate group from phosphoenolpyruvate to a given sugar the phosphoryl group is sequentially transferred from one protein to another. Expand
Genetic evidence for the role of a bacterial phosphotransferase system in sugar transport.
TLDR
It is concluded that the phosphotransferase system is intimately involved in sugar transport, and a single mutation in Salmonella typhimurium that results in an inability to grow on nine carbohydrates concomitant with a loss of enzyme I is concerned. Expand
Deletion Mapping of the Genes Coding for HPr and Enzyme I of the Phosphoenolpyruvate: Sugar Phosphotransferase System in Salmonella typhimurium
TLDR
A hypothesis is presented for a mechanism of deletion formation and the structural genes coding for HPr and Enzyme I are shown to be cotransducible in Salmonella typhimurium. Expand
Promoter-Like Mutation Affecting HPr and Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System in Salmonella typhimurium
A promoter-like mutation, ptsP160, has been identified which drastically reduces expression of the genes specifying two proteins, HPr and enzyme I, of the phosphoenolpyruvate:sugar phosphotransferaseExpand
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