Biochemical and Biophysical Research Communications
Regular ArticlePurification and Characterization of the Periplasmic Domain of EnvZ Osmosensor inEscherichia coli
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Cited by (15)
Identification of transmembrane helix 1 (TM1) surfaces important for EnvZ dimerisation and signal output
2016, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :In most cases, OmpK35, which belongs to the OmpF porin family that has a larger channel size, was replaced with OmpK36, which belongs to the OmpC family and possesses a smaller channel size [4]. EnvZ of Escherichia coli is a canonical sensor histidine kinase (SHK) that responds to changes in the extracellular osmolarity of inner-membrane impermeable compounds such as sucrose, or the presence of certain lipophilic compounds, e.g. procaine, by modulating the intracellular level of phosphorylated OmpR, its cognate response regulator (RR) (Fig. 1A) [14–17]. Subsequently, phospho-OmpR regulates the transcription of a number of genes, including those encoding two major outer membrane porins, OmpF and OmpC.
Structural characterization of AS1-membrane interactions from a subset of HAMP domains
2011, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :The two other HAMP domains are from receptors, Af1503 and EnvZEc, whose mechanism of stimulus detection is not well understood. In addition, structural predictions of these receptors [60,61] do not possess the periplasmic four-helix bundle shared by NarXEc and TarEc. The helix-interaction model [6] proposes that the amphipathic nature of AS1 should allow it to align parallel to the membrane, with its hydrophobic face in contact with the hydrophobic interior of the phospholipid bilayer and its positively charged residues in association with the polar headgroups (Figs. 7B and S1).
Functional and Structural Characterization of EnvZ, an Osmosensing Histidine Kinase of E. coli
2007, Methods in EnzymologyCitation Excerpt :EnvZ, an osmosensor histidine kinase, is a multidomain transmembrane protein which consists of 450 amino acid residues which obligatorily form a dimer in the inner membrane. Earlier studies on EnvZ showed that it contains a short N‐terminal cytoplasmic tail (residues 1–15), two transmembrane segments, TM1 (residues 16–47) and TM2 (residues 163–179) (Forst et al., 1987), a periplasmic receptor domain (residues 48–162) (Egger and Inouye, 1997; Khorchid et al., 2005), and a cytoplasmic C‐terminal domain (residues 180–450). Biochemical studies demonstrated that using ATP, EnvZ can autophosphorylate its conserved His residue, His243 (Roberts et al., 1994).
A novel regulatory cascade involving bluR, ycgZ, and lon controls the expression of Escherichia coli OmpF porin
2017, Frontiers in MicrobiologyStimulus Perception by Histidine Kinases
2016, Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria
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