Structural characterization of <i>Escherichia coli</i> sensor histidine kinase EnvZ: the periplasmic C-terminal core domain is critical for homodimerization

Khorchid, Ahmad; Inouye, Masayori; Ikura, Mitsuhiko

doi:10.1042/bj20041125

Cited by 18 publications

(13 citation statements)

References 38 publications

(37 reference statements)

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“… Mutations are depicted on a representation of EnvZ dimer, based on the transmembrane/periplasmic domain model [ 47 ] and the NMR structures of the homodimeric core [ 48 ] and the ATP-binding domain [ 49 ] with ATP bound molecules depicted in balls and sticks. Localizations of the amino acid where mutations had been identified are represented by red stars (linker and periplasmic domain) and with red side chain in the known EnvZ sub-structures.…”

Section: Resultsmentioning

confidence: 99%

Dissecting the Genetic Components of Adaptation of Escherichia coli to the Mouse Gut

et al. 2008

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While pleiotropic adaptive mutations are thought to be central for evolution, little is known on the downstream molecular effects allowing adaptation to complex ecologically relevant environments. Here we show that Escherichia coli MG1655 adapts rapidly to the intestine of germ-free mice by single point mutations in EnvZ/OmpR two-component signal transduction system, which controls more than 100 genes. The selective advantage conferred by the mutations that modulate EnvZ/OmpR activities was the result of their independent and additive effects on flagellin expression and permeability. These results obtained in vivo thus suggest that global regulators may have evolved to coordinate activities that need to be fine-tuned simultaneously during adaptation to complex environments and that mutations in such regulators permit adjustment of the boundaries of physiological adaptation when switching between two very distinct environments.

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Section: Resultsmentioning

confidence: 99%

Dissecting the Genetic Components of Adaptation of Escherichia coli to the Mouse Gut

et al. 2008

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“…It has long been known that bacterial chemoreceptors, such as Tar and Tsr, exist in dimeric form on the cell surface . The same is true for the Escherichia coli extracellular osmolarity sensor EnvZ .…”

Section: A Variety Of Receptors Exist In Dimeric Form Prior To Ligandmentioning

confidence: 96%

Activation of transmembrane cell‐surface receptors via a common mechanism? The “rotation model”

Maruyama

2015

BioEssays

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It has long been thought that transmembrane cell‐surface receptors, such as receptor tyrosine kinases and cytokine receptors, among others, are activated by ligand binding through ligand‐induced dimerization of the receptors. However, there is growing evidence that prior to ligand binding, various transmembrane receptors have a preformed, yet inactive, dimeric structure on the cell surface. Various studies also demonstrate that during transmembrane signaling, ligand binding to the extracellular domain of receptor dimers induces a rotation of transmembrane domains, followed by rearrangement and/or activation of intracellular domains. The paper here describes transmembrane cell‐surface receptors that are known or proposed to exist in dimeric form prior to ligand binding, and discusses how these preformed dimers are activated by ligand binding.

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“…The K6 residue in strain K-12 is also well conserved and may be involved in protein dimerization. The P41 EnvZ residue is in the periplasmic domain (flanking the membrane-spanning segment TM1) of the protein, which may be involved in fine-tuning osmotic signal transduction through dimerization of EnvZ, and it is adjacent to a predicted well- conserved alpha helix (33,85). The P41 residue is also well conserved, and mutations affecting this residue (P41L, P41S) in K-12-derived strains yield a protein that appears to be defective in its phosphatase activity, leading to a higher concentration of OmpR-P, thereby causing an OmpF-deficient, OmpCconstitutive phenotype (79).…”

Section: Vol 193 2011mentioning

confidence: 99%

Altered Regulation of the OmpF Porin by Fis inEscherichia coliduring an Evolution Experiment and between B and K-12 Strains

et al. 2011

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The phenotypic plasticity of global regulatory networks provides bacteria with rapid acclimation to a wide range of environmental conditions, while genetic changes in those networks provide additional flexibility as bacteria evolve across long time scales. We previously identified mutations in the global regulator-encoding gene fis that enhanced organismal fitness during a long-term evolution experiment with Escherichia coli. To gain insight into the effects of these mutations, we produced two-dimensional protein gels with strains carrying different fis alleles, including a beneficial evolved allele and one with an in-frame deletion. We found that Fis controls the expression of the major porin-encoding gene ompF in the E. coli B-derived ancestral strain used in the evolution experiment, a relationship that has not been described before. We further showed that this regulatory connection evolved over two different time scales, perhaps explaining why it was not observed before. On the longer time scale, we showed that this regulation of ompF by Fis is absent from the more widely studied K-12 strain and thus is specific to the B strain. On a shorter time scale, this regulatory linkage was lost during 20,000 generations of experimental evolution of the B strain. Finally, we mapped the Fis binding sites in the ompF regulatory region, and we present a hypothetical model of ompF expression that includes its other known regulators.

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Structural characterization of Escherichia coli sensor histidine kinase EnvZ: the periplasmic C-terminal core domain is critical for homodimerization

Cited by 18 publications

References 38 publications

Dissecting the Genetic Components of Adaptation of Escherichia coli to the Mouse Gut

Dissecting the Genetic Components of Adaptation of Escherichia coli to the Mouse Gut

Activation of transmembrane cell‐surface receptors via a common mechanism? The “rotation model”

Altered Regulation of the OmpF Porin by Fis inEscherichia coliduring an Evolution Experiment and between B and K-12 Strains

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