Glucose transport in Escherichia coli

Erni, Bernhard

doi:10.1016/0168-6445(89)90004-1

Cited by 33 publications

(24 citation statements)

References 63 publications

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“…Kofoid and Parkinson (11, lla) showed that a stretch of 209 residues at the C terminus of EIIGic exhibits a sequence similarity of 39% with the transmitter consensus motif of sensor proteins that they defined. Consistent with the properties expected for a transmitter module, the C-terminal end of EIIGIc comprising about 90 residues has hydrophilic properties, and biochemical experiments suggest that this region might be exposed at the cytoplasmic face of the membrane (8). These observations argue in favor of the notion that the membranebound EIIGIc might be a sensor protein resembling those of the two-component systems.…”

Section: Discussionsupporting

confidence: 65%

Positive regulation of the pts operon of Escherichia coli: genetic evidence for a signal transduction mechanism

Reuse

Danchin

1991

J Bacteriol

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The pts operon of Escherichia coli is composed of the genes ptsH, ptsI, and crr, which code for three proteins of the phosphoenolpyruvate-dependent phosphotransferase system (PTS): the HPr, enzyme I (EI), and EIIIGIC proteins, respectively. These three genes are organized in a complex operon in which the major part of expression of the distal gene, crr, is initiated from a promoter region within ptsl. Expression from the promoter region of the ptsH and ptsl genes has been studied in vivo by using gene fusions with lacZ. Transcription from this promoter region is under the positive control of catabolite activator protein (CAP)-cyclic AMP (cAMP) and is also enhanced during growth in the presence of glucose (a PTS substrate). This report describes a genetic characterization of the mechanism by which growth on glucose causes transcriptional stimulation of the pts operon. This regulation is dependent on transport through the glucose-specific permease of the PTS, EIIGiC.Our results strongly suggest that transcriptional regulation of the pts operon is the consequence of an increase in the level of unphosphorylated EIIGIC which is produced during glucose transport. Furthermore, overproduction of EIIGIC in the absence of transport was found to stimulate expression of the pts operon. We also observed that CAP-cAMP could cause stimulation independently of the EIIGIC and that glucose could activate in the absence of cAMP in a strain overproducing ETIGiC. Our results indicate that glucose acts like an environmental signal through a mechanism of signal transduction. A sequence similarity between the C terminus of EUG'C and the consensus of transmitter modules of the sensor proteins defined by E. C. Kofoid and J. S. Parkinson (Proc. Natl. Acad. Sci. USA 85: [4981][4982][4983][4984][4985] 1988) suggests that EUGiC might have properties in common with the sensors of the two-component systems.The phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS) catalyzes uptake and phosphorylation of a large number of carbohydrates in many different bacteria (for reviews, see references 19, 20, and 22). This system involves sequential phosphoryl group transfer events. The phosphoryl group of the donor molecule, PEP, is transferred to a series of PTS proteins and finally to the transported PTS carbohydrate. In Escherichia coli, two of these proteins are common to almost all PTS carbohydrates. Other proteins (at least 20) are specific for one or a few PTS carbohydrates. The two common proteins, HPr and enzyme I (El), encoded by the ptsH and ptsI genes, respectively, are cytoplasmic. The specific PTS proteins are either cytoplasmic phosphoproteins or membrane-bound permeases.Glucose is one of the PTS carbohydrates. Its transport requires, in addition to El and HPr, either of two other sets of specific proteins. The major part of glucose transport is mediated by the cytoplasmic enzyme EIIIGlC, encoded by the crr gene, and the glucose-specific permease, EIIG'C, encoded by the ptsG gene. EIIGIC is phosphorylated on a His residue by ...

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Section: Discussionsupporting

confidence: 65%

Positive regulation of the pts operon of Escherichia coli: genetic evidence for a signal transduction mechanism

Reuse

Danchin

1991

J Bacteriol

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“…Two-dimensional NMR studies have established the validity of this conclusion, showing that this N-terminal region of the HAgkC domain is highly mobile, exhibiting essentially unrestricted intramolecular motion (Stone et al, 1992). Interdomain Q-linkers and alanine/ proline-rich hinges that occur in the boundaries of functionally and structurally distinct but otherwise interacting domains of other PTS permeases have also been identified (Erni, 1989;Sutrina et al, 1990;Wu et al, 1990). The sequences depicted in Figure 4 reveal that all protein members of the Enzyme I family contain putative Q-linkers at the ends of regions I11 shown in Figure 3.…”

Section: Putative Flexible Linkers In Enzyme I Family Proteinsmentioning

confidence: 88%

Sequence analyses and evolutionary relationships among the energy‐coupling proteins enzyme I and HPr of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system

et al. 1993

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We have previously reported the overexpression, purification, and biochemical properties of the Bacillus subtilis Enzyme I of the phosphoeno1pyruvate:sugar phosphotransferase system (PTS) (Reizer, J., et al., 1992, J. Biol. Chem. 267,9158-9169). We now report the sequencing of thepfsl gene of B. subtilis encoding Enzyme I (570 amino acids and 63,076 Da). Putative transcriptional regulatory signals are identified, and the p f s operon is shown to be subject to carbon source-dependent regulation. Multiple alignments of the B. subtilis Enzyme I with (1) six other sequenced Enzymes I of the PTS from various bacterial species, (2) phosphoenolpyruvate synthase of Escherichia coli, and (3) bacterial and plant pyruvate:phosphate dikinases (PPDKs) revealed regions of sequence similarity as well as divergence. Statistical analyses revealed that these three types of proteins comprise a homologous family, and the phylogenetic tree of the 1 1 sequenced protein members of this family was constructed. This tree was compared with that of the 12 sequenced HPr proteins or protein domains. Antibodies raised against the B. subtilis and E. coli Enzymes I exhibited immunological cross-reactivity with each other as well as with PPDK of Bacferoides syrnbiosus, providing support for the evolutionary relationships of these proteins suggested from the sequence comparisons. Putative flexible linkers tethering the N-terminal and the C-terminal domains of protein members of the Enzyme I family were identified, and their potential significance with regard to Enzyme I function is discussed. The codon choice pattern of the B. subtilis and E, coliptsl andptsH genes was found to exhibit a bias toward optimal codons in these organisms. Quantitative analysis of this bias indicated that theptsHgenes have higher bias toward codons favored in highly expressed genes than the p t s l genes, in agreement with their relative levels of expression.

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“…The bacterial uptake of unlabeled glucose in E. coli occurs by active transport across the IM. Here, glucose molecules are bound to the periplasmic permease(s), then translocated and phosphorylated at the C6 atom, and released into the cytoplasm (50). The uptake of NBDG was proven to be specifically mediated by the phosphoenolpyruvate phosphotransferase system (51).…”

Section: Fluorescent Substratesmentioning

confidence: 99%

Viability states of bacteria—Specific mechanisms of selected probes

2010

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Single cell techniques like flow cytometry combined with viability staining can help to obtain information on viability states of bacteria. Many fluorescent dyes are available for this purpose and can be chosen according to the available excitation source, the species used, and the background of scientific questions and relevant specifications. Within this short overview, we focus on two diverse groups of bacteria: the gram2 Escherichia coli and representatives of the gram+ Mycobacterium to demonstrate differences and similarities in dye uptake principles, processing and binding. We call for attention to possible diverse responses of different species to various viability assays. The cell surface structure of bacteria and the chemical properties of fluorescent probes considerably determine the success of a certain staining practice. Particular focus was drawn on analysis of membrane integrity, uptake of substrates and transformation of fluorogenic substrates. '

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Glucose transport in Escherichia coli

Abstract: 13J.3. The glucose perm eases of E. coli E. coli and S. typhimurium both have two glucose-specific permeases. One, the glucose permease proper, is specific for glucose and the non-0168-6445/89/$03.50

Cited by 33 publications

References 63 publications

Positive regulation of the pts operon of Escherichia coli: genetic evidence for a signal transduction mechanism

Positive regulation of the pts operon of Escherichia coli: genetic evidence for a signal transduction mechanism

Sequence analyses and evolutionary relationships among the energy‐coupling proteins enzyme I and HPr of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system

Viability states of bacteria—Specific mechanisms of selected probes

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