EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes

Russo, Frank D.; Silhavy, Thomas J.

doi:10.1016/0022-2836(91)90497-t

Cited by 187 publications

(190 citation statements)

References 38 publications

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“…Nevertheless, it is tempting to speculate that CbnK acts as a peptide pheromone sensor involved in regulation of CbnR activity, probably by modulation of its phosphorylation state. The results described here would then suggest that CbnK maintains CbnR in a non-activated form under non inducing conditions, which has been reported for other response regulators [2,23,28].…”

Section: Cs and Cb2 Control Cbn Promoter Activity Via Cbnk And Cbnrsupporting

confidence: 81%

A two-component signal-transduction cascade in Carnobacterium piscicola LV17B: two signaling peptides and one sensor-transmitter

et al. 2001

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A two-component signal-transduction cascade in Carnobacterium piscicola LV17B Kleerebezem, M; Kuipers, Oscar; de Vos, WM; Stiles, ME; Quadri, LEN; Vos, Willem M. de; Stiles, Michael E.; Quadri, Luis E.N. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. AbstractIn the lactic acid bacterium Carnobacterium piscicola LV17B a peptide-pheromone dependent quorum-sensing mode is involved in the regulation of bacteriocin production. Bacteriocin CB2 was identified as an environmental signal that induces bacteriocin production. Here, we demonstrate that a second 24 amino acid peptide (CS) also induces bacteriocin production. Transcription activation of several carnobacteriocin operons is triggered by CB2 or CS via a two-component signal transduction system composed of CbnK and CbnR.

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Section: Cs and Cb2 Control Cbn Promoter Activity Via Cbnk And Cbnrsupporting

confidence: 81%

A two-component signal-transduction cascade in Carnobacterium piscicola LV17B: two signaling peptides and one sensor-transmitter

et al. 2001

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“…pFR29* is a derivative of pFR29 from which the envZ gene has been excised (25). The plasmids were used to transform strains MH225.101 and MH513.101.…”

Section: Methodsmentioning

confidence: 99%

The Linker Region Plays an Important Role in the Interdomain Communication of the Response Regulator OmpR

Mattison¹,

Oropeza²,

Kenney

2002

Journal of Biological Chemistry

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OmpR is the response regulator of a two-component regulatory system that controls the expression of the porin genes ompF and ompC in Escherichia coli. This regulator consists of two domains joined by a flexible linker region. The amino-terminal domain is phosphorylated by the sensor kinase EnvZ, and the carboxylterminal domain binds DNA via a winged helix-turn-helix motif. In vitro studies have shown that amino-terminal phosphorylation enhances the DNA binding affinity of OmpR and, conversely, that DNA binding by the carboxyl terminus increases OmpR phosphorylation. In the present work, we demonstrate that the linker region contributes to this communication between the two domains of OmpR. Changing the specific amino acid composition of the linker alters OmpR function, as does increasing or decreasing its length. Three linker mutants give rise to an OmpF ؉ OmpC ؊ phenotype, but the defects are not due to a shared molecular mechanism. Currently, functional homology between response regulators is predicted based on similarities in the amino and carboxylterminal domains. The results presented here indicate that linker length and composition should also be considered. Furthermore, classification of response regulators in the same subfamily does not necessarily imply that they share a common response mechanism.

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“…The EnvZ/OmpR system is a prototypical TCS in which EnvZ senses changes in environmental osmolality and transmits the signal to its response regulator, OmpR. OmpR is a transcription factor that regulates the transcription of the outer-membrane porin genes ompF and ompC (6)(7)(8)(9)(10)(11)(12)(13)(14)(15). Phosphorylation of OmpR changes its affinity for promoters of outer membrane porin genes, resulting in altered porin expression (16).…”

Section: Introductionmentioning

confidence: 99%

Lipid-Mediated Regulation of Embedded Receptor Kinases via Parallel Allosteric Relays

Ghosh

Wang

Ramesh

et al. 2017

Biophysical Journal

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Membrane-anchored receptors are essential cellular signaling elements for stimulus sensing, propagation, and transmission inside cells. However, the contributions of lipid interactions to the function and dynamics of embedded receptor kinases have not been described in detail. In this study, we used amide hydrogen/deuterium exchange mass spectrometry, a sensitive biophysical approach, to probe the dynamics of a membrane-embedded receptor kinase, EnvZ, together with functional assays to describe the role of lipids in receptor kinase function. Our results reveal that lipids play an important role in regulating receptor function through interactions with transmembrane segments, as well as through peripheral interactions with nonembedded domains. Specifically, the lipid membrane allosterically modulates the activity of the embedded kinase by altering the dynamics of a glycine-rich motif that is critical for phosphotransfer from ATP. This allostery in EnvZ is independent of membrane composition and involves direct interactions with transmembrane and periplasmic segments, as well as peripheral interactions with nonembedded domains of the protein. In the absence of the membrane-spanning regions, lipid allostery is propagated entirely through peripheral interactions. Whereas lipid allostery impacts the phosphotransferase function of the kinase, extracellular stimulus recognition is mediated via a four-helix bundle subdomain located in the cytoplasm, which functions as the osmosensing core through osmolality-dependent helical stabilization. Our findings emphasize the functional modularity in a membrane-embedded kinase, separated into membrane association, phosphotransferase function, and stimulus recognition. These components are integrated through long-range communication relays, with lipids playing an essential role in regulation.

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EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes

Cited by 187 publications

References 38 publications

A two-component signal-transduction cascade in Carnobacterium piscicola LV17B: two signaling peptides and one sensor-transmitter

A two-component signal-transduction cascade in Carnobacterium piscicola LV17B: two signaling peptides and one sensor-transmitter

The Linker Region Plays an Important Role in the Interdomain Communication of the Response Regulator OmpR

Lipid-Mediated Regulation of Embedded Receptor Kinases via Parallel Allosteric Relays

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