Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli.

Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli. Abstract Text:

Ryuta Kishii,Liliana Falzon,Takeshi Yoshida,Hiroshi Kobayashi,Masayori Inouye,

The HAMP domain plays an essential role in signal transduction not only in histidine kinase but also in a number of other signal-transducing receptor proteins. Here we expressed the EnvZ HAMP domain (Arg(180)-Thr(235)) with the R218K mutation (termed L(RK)) or with L(RK) connected with domain A (Arg(180)-Arg(289)) (termed LA(RK)) of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli, by fusing it with protein S. The L(RK) and LA(RK) proteins were purified after removing protein S. The CD analysis of the isolated L protein revealed that it consists of a random structure or is unstructured. This suggests that the EnvZ HAMP domain by itself is unable to form a stable structure and that this structural fragility may be important for its role in signal transduction. Interestingly the substitution of Ala(193) in the EnvZ HAMP domain with valine or leucine in Tez1A1, a chimeric protein of Tar and EnvZ, caused a constitutive OmpC phenotype. The CD analysis of LA(RK)(A193L) revealed that this mutated HAMP domain possesses considerable secondary structures and that the thermostability of this entire LA(RK)(A193L) became substantially lower than that of LA(RK) or just domain A, indicating that the structure of the HAMP domain with the A193L mutation affects the stability of downstream domain A. This results in cooperative thermodenaturation of domain A with the mutated HAMP domain. These results are discussed in light of the recently solved NMR structure of the HAMP domain from a thermophilic bacterium (Hulko, M., Berndt, F., Gruber, M., Linder, J. U., Truffault, V., Schultz, A., Martin, J., Schultz, J. E., Lupas, A. N., and Coles, M. (2006) Cell 126, 929-940).

Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli. Publishing Authors By Initials

R Kishii,L Falzon,T Yoshida,H Kobayashi,M Inouye,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research

PUBMED ID PMID:

MEDLINE DATE:

Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 26401-8

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 16

MONTH: 07

YEAR: 2007

Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli. Keywords Mesh Terms:

KEYWORDS: Structure-Activity Relationship

MESH TERMS: physiology

Chemical & Substance for Abstract: Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli. Information

Substance Name: protein-histidine kinase

Registry Number: EC 2.7.3.-

Grant and Affiliation Information for Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli.

AFFILIATION: Discovery Research Laboratories, Kyorin Pharmaceutical Co., Ltd., Shimotsuga, Tochigi 329-0114, Japan.

Country: United States

AGENCY: United States NIGMS

GRANT: GM076587A

ACRONYM: GM

MEDLINETA: J Biol Chem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli Related Publications

• A new method for the extracellular production of recombinant thermolysin by co-expressing the mature sequence and pro-sequence in Escherichia coli.
• Artificial DNAs based on alkynyl C-nucleosides as a superior scaffold for homo- and heteroexcimer emissions.
• Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E.
• Bacterial bioreactors for high yield production of recombinant protein.
• Cerebral perfusion changes in older delirious patients using 99mTc HMPAO SPECT.
• Characteristics associated with delirium in older patients in a medical intensive care unit.
• Depressive symptoms and the risk of incident delirium in older hospitalized adults.
• Dissection of 16S rRNA methyltransferase (KsgA) function in Escherichia coli.
• Does educational attainment contribute to risk for delirium? A potential role for cognitive reserve.
• Effects of site-directed mutagenesis of the surface residues Gln128 and Gln225 of thermolysin on its catalytic activity.
• Functional and Structural Characterization of EnvZ, an Osmosensing Histidine Kinase of E. coli.
• Identification of intracellular localization signals and of mechanisms underlining the nucleocytoplasmic shuttling of human aryl hydrocarbon receptor repressor.
• Improving the activity and stability of thermolysin by site-directed mutagenesis.
• Kinetic analysis of the activation-and-inhibition dual effects of cobalt ion on thermolysin activity.
• Molecular mechanism of the inhibitory effect of cobalt ion on thermolysin activity and the suppressive effect of calcium ion on the cobalt ion-dependent inactivation of thermolysin.
• NBK/BIK antagonizes MCL-1 and BCL-XL and activates BAK-mediated apoptosis in response to protein synthesis inhibition.
• Orthologous gene of beetle luciferase in non-luminous click beetle, Agrypnus binodulus (Elateridae), encodes a fatty acyl-CoA synthetase.
• Photooxygenation of alkynylperylenes. Formation of dibenzo[jk,mn]phenanthrene-4,5-diones.
• Real-time bioluminescence imaging of a protein secretory pathway in living mammalian cells using Gaussia luciferase.
• Recognizing delirium superimposed on dementia: assessing nurses' knowledge using case vignettes.
• Serum biomarkers for delirium.
• Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli.
• Studies on monoterpene glucosides and related natural products.
• Study of superoxide dismutase's expression in the colon produced by azoxymethane and inositol hexaphosfate's paper, in mice.
• Temporal profile of circadian clock gene expression in a transplanted suprachiasmatic nucleus and peripheral tissues.
• The Design and Development of Tar-EnvZ Chimeric Receptors.
• The Inhibitory Effect of Aryl Hydrocarbon Receptor Repressor (AhRR) on the Growth of Human Breast Cancer MCF-7 Cells.
• The role of neuroimaging in elucidating delirium pathophysiology.
• Two New Iridoid Glucosides of Plantago asiatica.
• Use of a computer-based reminder to improve sedative-hypnotic prescribing in older hospitalized patients.