Elucidation of a PTS–Carbohydrate Chemotactic Signal Pathway in<i>Escherichia coli</i>Using a Time-resolved Behavioral Assay

Lux, Renate; Munasinghe, V. Ranjit N.; Castellano, Fred; Lengeler, Joseph W.; Corrie, John E. T.; Khan, Shahid

doi:10.1091/mbc.10.4.1133

Cited by 55 publications

(43 citation statements)

References 60 publications

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“…It was established that chemotaxis towards PTS sugars at relatively high concentrations (Ͼ1 mM) is also mediated by the chemoreceptors Aer and Tsr (296), which sense redox state and proton motive force, respectively (865). In E. coli, chemotaxis by PTS sugars can be abolished by knocking out CheA, CheY, CheW, EI, HPr, or the corresponding sugar-specific EII complexes, whereas the removal of the MCPs, CheR, or CheB has no significant effect (8,297,460,462,498,550,609,641,745,863,864; see also reference 678). Despite the fact that PTS-mediated sugar uptake and Che protein-mediated chemotaxis involve similar phosphoryl transfer reactions, no phosphoryl transfer between PTS components and Che proteins has been demonstrated (379).…”

mentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,202

769

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SUMMARY The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

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mentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,202

769

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“…(Lux et al 1999). This scheme is not applicable for B. subtilis as the dephosphorylation of CheY would lead to tumbling.…”

Section: Discussion About Mcpsmentioning

confidence: 99%

Comparative structural bioinformatics analysis of Bacillus amyloliquefaciens chemotaxis proteins within Bacillus subtilis group

Yssel

Reva

Bishop

2011

Appl Microbiol Biotechnol

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Chemotaxis is a process in which bacteria sense their chemical environment and move towards more favourable conditions. Since plant colonization by bacteria is a multifaceted process which requires a response to the complex chemical environment, a finely tuned and sensitive chemotaxis system is needed. Members of the Bacillus subtilis group including Bacillus amyloliquefaciens are industrially important, for example in bio-pesticides. The group exhibits plant growth promoting characteristics, with different specificity towards certain host plants. Therefore, we hypothesize that while the principal molecular mechanisms of bacterial chemotaxis may be conserved, the bacterial chemotaxis system may need an evolutionary tweaking to adapt it to specific requirements, particularly in the process of evolution of free-living soil organisms, towards plant colonization behaviour. To date almost nothing is known about what parts of the chemotaxis proteins are subjected to positive amino acid substitutions, involved in adjusting the chemotaxis system of bacteria during speciation.In this novel study, positively selected and purified sites of chemotaxis proteins were calculated and these residues were mapped onto homology models that were built for the chemotaxis proteins, in an attempt to understand the spatial evolution of the chemotaxis proteins. Various positively selected amino acids were identified in semi-conserved regions of the proteins away from the known active sites.

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“…The dephosphorylated state of EIIA component, which is predominant during active uptake of the PTS dependent substrates, correlates with low PrfA activity and vice versa (46). Second, in E. coli, dephosphorylated EI, at a high glucose level, inhibits the chemotaxis protein, CheA, changing the motility pattern of the cell in such a way that it is able to approach the source of food (47). Not only that, but the cAMP-independent catabolite repression control protein Crc of P. aeruginosa is necessary for the formation of biofilm (48).…”

Section: Role Of Ccr Machinery Beyond Sugar Metabolismmentioning

confidence: 99%

Rewiring carbon catabolite repression for microbial cell factory

Parisutham¹,

Kim²,

Lee³

et al. 2012

BMB Reports

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Carbon catabolite repression (CCR) is a key regulatory system found in most microorganisms that ensures preferential utilization of energy-efficient carbon sources. CCR helps microorganisms obtain a proper balance between their metabolic capacity and the maximum sugar uptake capability. It also constrains the deregulated utilization of a preferred cognate substrate, enabling microorganisms to survive and dominate in natural environments. On the other side of the same coin lies the tenacious bottleneck in microbial production of bioproducts that employs a combination of carbon sources in varied proportion, such as lignocellulose-derived sugar mixtures. Preferential sugar uptake combined with the transcriptional and/or enzymatic exclusion of less preferred sugars turns out one of the major barriers in increasing the yield and productivity of fermentation process. Accumulation of the unused substrate also complicates the downstream processes used to extract the desired product. To overcome this difficulty and to develop tailor-made strains for specific metabolic engineering goals, quantitative and systemic understanding of the molecular interaction map behind CCR is a prerequisite. Here we comparatively review the universal and strain-specific features of CCR circuitry and discuss the recent efforts in developing synthetic cell factories devoid of CCR particularly for lignocellulose-based biorefinery. [BMB reports 2012; 45(2): 59-70]

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Elucidation of a PTS–Carbohydrate Chemotactic Signal Pathway inEscherichia coliUsing a Time-resolved Behavioral Assay

Cited by 55 publications

References 60 publications

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Comparative structural bioinformatics analysis of Bacillus amyloliquefaciens chemotaxis proteins within Bacillus subtilis group

Rewiring carbon catabolite repression for microbial cell factory

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