Control of <i>Bacillus subtilis mtl</i> operon expression by complex phosphorylation‐dependent regulation of the transcriptional activator MtlR

Joyet, Philippe; Derkaoui, Meriem; Poncet, Sandrine; Deutscher, Josef

doi:10.1111/j.1365-2958.2010.07175.x

Cited by 44 publications

(92 citation statements)

References 64 publications

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“…2). In contrast, induction of the mannitol operon of B. subtilis, which is controlled by the transcription activator MtlR, occurs only when the PϳEIIA Mtl -mediated phosphorylation of MtlR at the conserved cysteyl residue in the penultimate EIIB Gat -like domain is prevented by the presence of mannitol in the growth medium (58). So far, B. subtilis MtlR is the only example of PϳEIIA-mediated phosphorylation of a transcription activator at the conserved Cys in the EIIB Gat -like domain (Fig.…”

Section: Proteins Containing a Pts Component Fused To The N Or C Termmentioning

confidence: 99%

“…Although the surrounding of the phosphorylatable His of EIIA Glc is nicely conserved in DcuA (GVELFVHFG in EIIA Glc and GVALA VCFG in DcuA), the His itself is replaced with a Cys. However, Cys residues are also sometimes used as phosphorylation sites in PTS proteins (EIIB domain) and also in at least one PTS-controlled transcription activator (58). It is therefore tempting to assume that the DcuA transport activity might be controlled via either phosphorylation by or interaction with HPr or the EIIB Glc domain of the glucose-specific PTS permease.…”

Section: Proteins Containing a Pts Component Fused To The N Or C Termmentioning

confidence: 99%

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The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions

Deutscher

Aké

Derkaoui

et al. 2014

Microbiol Mol Biol Rev

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352

374

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SUMMARY The bacterial phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS) carries out both catalytic and regulatory functions. It catalyzes the transport and phosphorylation of a variety of sugars and sugar derivatives but also carries out numerous regulatory functions related to carbon, nitrogen, and phosphate metabolism, to chemotaxis, to potassium transport, and to the virulence of certain pathogens. For these different regulatory processes, the signal is provided by the phosphorylation state of the PTS components, which varies according to the availability of PTS substrates and the metabolic state of the cell. PEP acts as phosphoryl donor for enzyme I (EI), which, together with HPr and one of several EIIA and EIIB pairs, forms a phosphorylation cascade which allows phosphorylation of the cognate carbohydrate bound to the membrane-spanning EIIC. HPr of firmicutes and numerous proteobacteria is also phosphorylated in an ATP-dependent reaction catalyzed by the bifunctional HPr kinase/phosphorylase. PTS-mediated regulatory mechanisms are based either on direct phosphorylation of the target protein or on phosphorylation-dependent interactions. For regulation by PTS-mediated phosphorylation, the target proteins either acquired a PTS domain by fusing it to their N or C termini or integrated a specific, conserved PTS regulation domain (PRD) or, alternatively, developed their own specific sites for PTS-mediated phosphorylation. Protein-protein interactions can occur with either phosphorylated or unphosphorylated PTS components and can either stimulate or inhibit the function of the target proteins. This large variety of signal transduction mechanisms allows the PTS to regulate numerous proteins and to form a vast regulatory network responding to the phosphorylation state of various PTS components.

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Section: Proteins Containing a Pts Component Fused To The N Or C Termmentioning

confidence: 99%

Section: Proteins Containing a Pts Component Fused To The N Or C Termmentioning

confidence: 99%

The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions

Deutscher

Aké

Derkaoui

et al. 2014

Microbiol Mol Biol Rev

Self Cite

352

374

View full text Add to dashboard Cite

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“…Several operons participating in catabolism of PTS sugars are controlled by regulators that contain a PRD [46]. PRDmediated regulation has been extensively studied for the Escherichia coli antiterminator BglG [47], B. subtilis antiterminator licT [48,49] and B. subtilis transcriptional regulator MtlR [50,51]. To assess the functional relationships between the PRD-containing transcriptional activator of S.iniae, GatR, and the above regulators from E. coli and B. subtilis, we conducted a domain correlation analysis ( Figure 2G).…”

Section: Eiicmentioning

confidence: 99%

“…One major difference is that MtlR possesses two PRDs (PRD1 and PRD2) while GatR only contains PRD2. In contrast to BglG and licT, MtlR from B. subtilis is activated via bacterial membrane sequestration mediated by its cognate membrane EIIB Mtl [50][51][52]. B. subtilis MtlR controls expression of the mtlAFD operon, which mediates the utilization of mannitol [51].…”

Section: Eiicmentioning

confidence: 99%

“…In contrast to BglG and licT, MtlR from B. subtilis is activated via bacterial membrane sequestration mediated by its cognate membrane EIIB Mtl [50][51][52]. B. subtilis MtlR controls expression of the mtlAFD operon, which mediates the utilization of mannitol [51]. In the absence of mannitol, intracellular P-EIIB Mtl prevails, which does not interact with MtlR [52].…”

Section: Eiicmentioning

confidence: 99%

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Comparative genome analysis of Streptococcus iniae DX09 reveals new insights into niche adaptation and competitive host colonisation ability

Liu¹,

Wang²,

Wang³

2017

Oncotarget

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Streptococcus iniae is a significant pathogen in a variety of marine and freshwater cultured fish species. Previous investigations on S. iniae have been limited to a single virulence gene or genome. However, different strains are associated with varying pathogenicity and niche adaptation properties. For comprehensive characterization of the genetic variations in S. iniae, whole-genome sequencing of S. iniae DX09 (isolated from diseased catfish) was performed and comparative genome analysis with eight S. iniae strains conducted to determine the virulence evolution patterns. Comparative analysis of all sequenced S. iniae revealed genome-genome variations, mainly in two plasticity zones, within genes encoding specific functions, such as the Ess/type VII secretion system and phosphoenolpyruvate-carbohydrate phosphotransferase system, reflecting adaptation to colonisation of specific host habitats. The plasticity zones analyzed in the S. iniae genome may be a paradigm rather than a unique combination of horizontal gene transfer and underlie the emergence of pathogenic Gram-positive bacteria.

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The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS): an interface between energy and signal transduction

Erni

2012

J IRAN CHEM SOC

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Control of Bacillus subtilis mtl operon expression by complex phosphorylation‐dependent regulation of the transcriptional activator MtlR

Abstract: Summary

Cited by 44 publications

References 64 publications

The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions

The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions

Comparative genome analysis of Streptococcus iniae DX09 reveals new insights into niche adaptation and competitive host colonisation ability

The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS): an interface between energy and signal transduction

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