Analysis of Ethylene Receptors: Assay for Histidine Kinase Activity

2017 ◽  
pp. 87-99
Author(s):  
G. Eric Schaller ◽  
Brad M. Binder
Keyword(s):  
Histidine Kinase ◽  
Kinase Activity ◽  
Ethylene Receptors

scholarly journals Histidine kinase MHZ1/OsHK1 interacts with ethylene receptors to regulate root growth in rice

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
He Zhao ◽  
Kai-Xuan Duan ◽  
Biao Ma ◽  
Cui-Cui Yin ◽  
Yang Hu ◽  
...  
Keyword(s):  
Root Growth ◽  
Histidine Kinase ◽  
Ethylene Receptors

scholarly journals Evidence for Serine/Threonine and Histidine Kinase Activity in the Tobacco Ethylene Receptor Protein NTHK2

2004 ◽  
Vol 136 (2) ◽  
pp. 2971-2981 ◽  
Author(s):  
Zhi-Gang Zhang ◽  
Hua-Lin Zhou ◽  
Tao Chen ◽  
Yan Gong ◽  
Wan-Hong Cao ◽  
...  
Keyword(s):  
Histidine Kinase ◽  
Kinase Activity ◽  
Receptor Protein ◽  
Ethylene Receptor

Histidine kinase activity and the regulation of ethylene signal transduction

2005 ◽  
Vol 83 (6) ◽  
pp. 563-570 ◽  
Author(s):  
Michael G Mason ◽  
G Eric Schaller
Keyword(s):  
Signal Transduction ◽  
Plant Growth ◽  
Histidine Kinase ◽  
Kinase Activity ◽  
Ethylene Receptor ◽  
Serine Threonine Kinase ◽  
Two Component ◽  
Ethylene Signal Transduction ◽  
Ethylene Signal

Ethylene is a gaseous hormone that regulates many aspects of plant growth and development. Although the effect of ethylene on plant growth was discovered a century ago, the key players in the ethylene response pathway were only identified over the last 15 years. In Arabidopsis, ethylene is perceived by a family of five receptors (ETR1, ETR2, ERS1, ERS2, and EIN4) that resemble two-component histidine kinases. Of these, only ETR1 and ERS1 contain all the conserved residues required for histidine kinase activity. The ethylene receptors appear to function primarily through CTR1, a serine/threonine kinase that actively suppresses ethylene responses in air (absence of ethylene). Despite recent progress toward understanding ethylene signal transduction, the role of the ethylene-receptor histidine-kinase activity remains unclear. This review considers the significance of histidine kinase activity in ethylene signaling and possible mechanisms by which it may modulate ethylene responses.Key words: ethylene receptor, ETR1, histidine kinase, two-component, phosphorylation, Arabidopsis.

scholarly journals Use of a semisynthetic epitope to probe histidine kinase activity and regulation

2010 ◽  
Vol 397 (2) ◽  
pp. 139-143 ◽  
Author(s):  
Hans K. Carlson ◽  
Lars Plate ◽  
Mark S. Price ◽  
Jasmina J. Allen ◽  
Kevan M. Shokat ◽  
...  
Keyword(s):  
Histidine Kinase ◽  
Kinase Activity

scholarly journals HAMP Domain Rotation and Tilting Movements Associated with Signal Transduction in the PhoQ Sensor Kinase

mBio ◽  
2015 ◽  
Vol 6 (3) ◽  
Author(s):  
Susana Matamouros ◽  
Kyle R. Hager ◽  
Samuel I. Miller
Keyword(s):  
Histidine Kinase ◽  
Kinase Activity ◽  
Catalytic Domain ◽  
Structural Information ◽  
Mechanistic Model ◽  
Full Length ◽  
Physical Interaction ◽  
Content Type ◽  
Serovar Typhimurium ◽  
Α Helix

ABSTRACTHAMP domains are α-helical coiled coils that often transduce signals from extracytoplasmic sensing domains to cytoplasmic domains. Limited structural information has resulted in hypotheses that specific HAMP helix movement changes downstream enzymatic activity. These hypotheses were tested by mutagenesis and cysteine cross-linking analysis of the PhoQ histidine kinase, essential for resistance to antimicrobial peptides in a variety of enteric pathogens. These results support a mechanistic model in which periplasmic signals which induce an activation state generate a rotational movement accompanied by a tilt in α-helix 1 which activates kinase activity. Biochemical data and a high-confidence model of the PhoQ cytoplasmic domain indicate a possible physical interaction of the HAMP domain with the catalytic domain as necessary for kinase repression. These results support a model of PhoQ activation in which changes in the periplasmic domain lead to conformational movements in the HAMP domain helices which disrupt interaction between the HAMP and the catalytic domains, thus promoting increased kinase activity.IMPORTANCEMost studies on the HAMP domain signaling states have been performed with chemoreceptors or the HAMP domain of Af1503. Full-length structures of the HAMP-containing histidine kinases VicK and CpxA or a hybrid between the HAMP domain of Af1503 and the EnvZ histidine kinase agree with the parallel four-helix bundle structure identified in Af1503 and provide snapshots of structural conformations experienced by HAMP domains. We took advantage of the fact that we can easily regulate the activation state of PhoQ histidine kinase to study its HAMP domain in the context of the full-length protein in living cells and provide biochemical evidence for different conformational states experienced bySalmonella entericaserovar Typhimurium PhoQ HAMP domain upon signaling.

scholarly journals Histidine kinase activity of the ETR1 ethylene receptor from Arabidopsis

1998 ◽  
Vol 95 (13) ◽  
pp. 7825-7829 ◽  
Author(s):  
R. L. Gamble ◽  
M. L. Coonfield ◽  
G. E. Schaller
Keyword(s):  
Histidine Kinase ◽  
Kinase Activity ◽  
Ethylene Receptor

scholarly journals SpdC, a novel virulence factor, controls histidine kinase activity in Staphylococcus aureus

2018 ◽  
Vol 14 (3) ◽  
pp. e1006917 ◽  
Author(s):  
Olivier Poupel ◽  
Caroline Proux ◽  
Bernd Jagla ◽  
Tarek Msadek ◽  
Sarah Dubrac
Keyword(s):  
Staphylococcus Aureus ◽  
Virulence Factor ◽  
Histidine Kinase ◽  
Kinase Activity

scholarly journals Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase ofStaphylococcus aureus

2018 ◽  
Author(s):  
Ian R. Monk ◽  
Nausad Shaikh ◽  
Stephanie L. Begg ◽  
Mike Gajdiss ◽  
Jean Y. H. Lee ◽  
...  
Keyword(s):  
Metal Binding ◽  
Histidine Kinase ◽  
Kinase Activity ◽  
Zinc Ion ◽  
Pas Domain ◽  
Amino Acid Residues ◽  
Ofstaphylococcus Aureus ◽  
Wild Type ◽  
Peptidoglycan Synthesis ◽  
Metal Ligand

ABSTRACTWalKR (YycFG) is the only essential two-component regulator in the human pathogenStaphylococcus aureus.WalKR regulates peptidoglycan synthesis, but this function alone appears not to explain its essentiality. To understand WalKR function we investigated a suppressor mutant that arose when WalKR activity was impaired; a single histidine to tryptophan substitution (H271Y) in the cytoplasmic Per-Arnt-Sim (PASCYT) domain of the histidine kinase WalK. Introduction of the WalKH271Ymutation into wild-typeS.aureusactivated the WalKR regulon. Structural analyses of the WalK PASCYTdomain revealed a hitherto unknown metal binding site, in which a zinc ion (Zn2+) was tetrahedrally-coordinated by four amino acid residues including H271. The WallkH271Ymutation abrogated metal binding, increasing WalK kinase activity and WalR phosphorylation. Thus, Zn2+-binding negatively regulates WalKR activity. Identification of a metal ligand sensed by the WalKR system substantially expands our understanding of this criticalS.aureusregulon.

scholarly journals The Potential Functional Roles of NME1 Histidine Kinase Activity in Neuroblastoma Pathogenesis

2020 ◽  
Vol 21 (9) ◽  
pp. 3319 ◽  
Author(s):  
Kevin Adam ◽  
Jacqueline Lesperance ◽  
Tony Hunter ◽  
Peter E. Zage
Keyword(s):  
Cell Migration ◽  
Histidine Kinase ◽  
Kinase Activity ◽  
Neuroblastoma Cell ◽  
Neuroblastoma Cells ◽  
Functional Roles ◽  
Patient Prognosis ◽  
Histidine Phosphorylation ◽  
Tumor In Childhood ◽  
Neuroblastoma Cell Lines

Neuroblastoma is the most common extracranial solid tumor in childhood. Gain of chromosome 17q material is found in >60% of neuroblastoma tumors and is associated with poor patient prognosis. The NME1 gene is located in the 17q21.3 region, and high NME1 expression is correlated with poor neuroblastoma patient outcomes. However, the functional roles and signaling activity of NME1 in neuroblastoma cells and tumors are unknown. NME1 and NME2 have been shown to possess histidine (His) kinase activity. Using anti-1- and 3-pHis specific monoclonal antibodies and polyclonal anti-pH118 NME1/2 antibodies, we demonstrated the presence of pH118-NME1/2 and multiple additional pHis-containing proteins in all tested neuroblastoma cell lines and in xenograft neuroblastoma tumors, supporting the presence of histidine kinase activity in neuroblastoma cells and demonstrating the potential significance of histidine kinase signaling in neuroblastoma pathogenesis. We have also demonstrated associations between NME1 expression and neuroblastoma cell migration and differentiation. Our demonstration of NME1 histidine phosphorylation in neuroblastoma and of the potential role of NME1 in neuroblastoma cell migration and differentiation suggest a functional role for NME1 in neuroblastoma pathogenesis and open the possibility of identifying new therapeutic targets and developing novel approaches to neuroblastoma therapy.

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