ArticleThe Biochemical journal2005
Structural characterization of Escherichia coli sensor histidine kinase EnvZ: the periplasmic C-terminal core domain is critical for homodimerization.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Functional Characterization of the Histidine Kinase BaeS Reveals Critical Residues for BaeSR-Dependent Stress Signaling inMicroorganisms · 2026Article
- Combination of Chromatographic Analysis and Chemometric Methods with Bioactivity Evaluation of the Antibacterial Properties ofAntibiotics (Basel, Switzerland) · 2024Article
- Activation of transmembrane cell-surface receptors via a common mechanism? The "rotation model".BioEssays : news and reviews in molecular, cellular and developmental biology · 2015Review
- Altered regulation of the OmpF porin by Fis in Escherichia coli during an evolution experiment and between B and K-12 strains.Journal of bacteriology · 2011Article
- Determination of the physiological dimer interface of the PhoQ sensor domain.Journal of molecular biology · 2008Article
- Dissecting the genetic components of adaptation of Escherichia coli to the mouse gut.PLoS genetics · 2008Article
- Stimulus perception in bacterial signal-transducing histidine kinases.Microbiology and molecular biology reviews : MMBR · 2006Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Escherichia coli EnvZ is a membrane sensor histidine kinase that plays a pivotal role in cell adaptation to changes in extracellular osmolarity. Although the cytoplasmic histidine kinase domain of EnvZ has been extensively studied, both biochemically and structurally, little is known about the structure of its periplasmic domain, which has been implicated in the mechanism underlying its osmosensing function. In the present study, we report the biochemical and biophysical characterization of the periplasmic region of EnvZ (Ala38-Arg162). This region was found to form a dimer in solution, and to consist of two well-defined domains: an N-terminal a-helical domain and a C-terminal core domain (Glu83-Arg162) containing both a-helical and b-sheet secondary structures. Our pull-down assays and analytical ultracentrifugation analysis revealed that dimerization of the periplasmic region is highly sensitive to the presence of CHAPS, but relatively insensitive to salt concentration, thus suggesting the significance of hydrophobic interactions between the homodimeric subunits. Periplasmic homodimerization is mediated predominantly by the C-terminal core domain, while a regulatory function may be attributed mainly to the N-terminal a-helical domain, whose mutations have been shown previously to produce a high-osmolarity phenotype.
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