Antibodies against CKI1RD, a receiver domain of the sensor histidine kinase in Arabidopsis thaliana: From antigen preparation to in planta immunolocalization

2014 ◽  
Vol 100 ◽  
pp. 6-15
Author(s):  
Petra Borkovcová ◽  
Blanka Pekárová ◽  
Martina Válková ◽  
Radka Dopitová ◽  
Břetislav Brzobohatý ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Histidine Kinase ◽  
In Planta ◽  
Sensor Histidine Kinase ◽  
Antigen Preparation ◽  
Receiver Domain

Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana

2011 ◽  
Vol 67 (5) ◽  
pp. 827-839 ◽  
Author(s):  
Blanka Pekárová ◽  
Tomáš Klumpler ◽  
Olga Třísková ◽  
Jakub Horák ◽  
Séverine Jansen ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Histidine Kinase ◽  
Binding Specificity ◽  
Sensor Histidine Kinase ◽  
Receiver Domain

scholarly journals Novel Family of Sensor Histidine Kinase Genes in Arabidopsis thaliana

2001 ◽  
Vol 42 (2) ◽  
pp. 231-235 ◽  
Author(s):  
Chiharu Ueguchi ◽  
Hiromi Koizumi ◽  
Tomomi Suzuki ◽  
Takeshi Mizuno
Keyword(s):  
Arabidopsis Thaliana ◽  
Histidine Kinase ◽  
Sensor Histidine Kinase

scholarly journals Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase fromArabidopsis thaliana

2017 ◽  
Vol 292 (42) ◽  
pp. 17525-17540 ◽  
Author(s):  
Olga Otrusinová ◽  
Gabriel Demo ◽  
Petr Padrta ◽  
Zuzana Jaseňáková ◽  
Blanka Pekárová ◽  
...  
Keyword(s):  
Histidine Kinase ◽  
Conformational Dynamics ◽  
Sensor Histidine Kinase ◽  
Receiver Domain ◽  
Key Factor

scholarly journals AHK5 mediates ETR1-initiated multistep phosphorelay in Arabidopsis

2021 ◽  
Author(s):  
Agnieszka Szmitkowska ◽  
Abigail Rubiato Cuyacot ◽  
Blanka Pekarova ◽  
Marketa Zdarska ◽  
Josef Houser ◽  
...  
Keyword(s):  
Root Growth ◽  
Molecular Mechanism ◽  
Histidine Kinase ◽  
Hormonal Control ◽  
Response Mechanism ◽  
In Planta ◽  
Changing Environment ◽  
Receiver Domain ◽  
Ethylene Response ◽  
Sessile Organisms

Plants, like other sessile organisms, need to sense many different signals, and in response to them, modify their developmental programs to be able to survive in a highly changing environment. The multistep phosphorelay (MSP) in plants is a good candidate for a response mechanism that integrates multiple signal types both environmental and intrinsic in origin. Recently, ethylene was shown to control MSP activity via the histidine kinase (HK) activity of ETHYLENE RESPONSE 1 (ETR1)1,2, but the underlying molecular mechanism still remains unclear. Here we show that although ETR1 is an active HK, its receiver domain (ETR1RD) is structurally and functionally unable to accept the phosphate from the phosphorylated His in the ETR1 HK domain (ETR1HK) to initiate the phosphorelay to ARABIDOPSIS HISTIDINE-CONTAINING PHOSPHOTRANSMITTERs (AHPs), the next link downstream members in MSP signaling. Instead, ETR1 interacts with another HK ARABIDOPSIS HISTIDINE KINASE 5 (AHK5) and transfers the phosphate from ETR1HK through the receiver domain of AHK5 (AHK5RD), and subsequently to AHP1, AHP2 and AHP3, independently of the HK activity of AHK5. We show that AHK5 is necessary for ethylene-initiated, but not cytokinin-initiated, MSP signaling in planta and that it thus mediates hormonal control of root growth.

scholarly journals Structural insights into the histidine-containing phosphotransfer protein and receiver domain of sensor histidine kinase suggest a complex model in the two-component regulatory system in Pseudomonas aeruginosa

IUCrJ ◽  
2020 ◽  
Vol 7 (5) ◽  
pp. 934-948
Author(s):  
Shao-Kang Chen ◽  
Hong-Hsiang Guan ◽  
Pei-Hsun Wu ◽  
Li-Ting Lin ◽  
Meng-Chun Wu ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Active Site ◽  
Histidine Kinase ◽  
Convex Surface ◽  
Complex Model ◽  
Phosphoryl Group ◽  
Chronic Infections ◽  
Sensor Histidine Kinase ◽  
Receiver Domain ◽  
Two Component

In Pseudomonas aeruginosa, an important opportunistic pathogen that causes numerous acute and chronic infections, the hybrid two-component system (TCS) regulates the swarming ability and biofilm formation with a multistep phosphorelay, and consists of hybrid-sensor histidine kinase (HK), histidine-containing phosphotransfer protein (Hpt) and response regulator (RR). In this work, two crystal structures of HptB and the receiver domain of HK PA1611 (PA1611REC) of P. aeruginosa have been determined in order to elucidate their interactions for the transfer of the phosphoryl group. The structure of HptB folds into an elongated four-helix bundle – helices α2, α3, α4 and α5, covered by the short N-terminal helix α1. The imidazole side chain of the conserved active-site histidine residue His57, located near the middle of helix α3, protrudes from the bundle and is exposed to solvent. The structure of PA1611REC possesses a conventional (β/α)5 topology with five-stranded parallel β-sheets folded in the central region, surrounded by five α-helices. The divalent Mg2+ ion is located in the negatively charged active-site cleft and interacts with Asp522, Asp565 and Arg567. The HptB–PA1611REC complex is further modeled to analyze the binding surface and interactions between the two proteins. The model shows a shape complementarity between the convex surface of PA1611REC and the kidney-shaped HptB with fewer residues and a different network involved in interactions compared with other TCS complexes, such as SLN1-R1/YPD1 from Saccharomyces cerevisiae and AHK5RD/AHP1 from Arabidopsis thaliana. These structural results provide a better understanding of the TCS in P. aeruginosa and could potentially lead to the discovery of a new treatment for infection.

Stable genetic transformation of Arabidopsis thaliana by Agrobacterium inoculation in planta

1994 ◽  
Vol 5 (4) ◽  
pp. 551-558 ◽  
Author(s):  
Seok So Chang ◽  
Soon Ki Park ◽  
Byung Chul Kim ◽  
Bong Joong Kang ◽  
Dal Ung Kim ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Genetic Transformation ◽  
In Planta

scholarly journals Ca2+-Dependent Protein Kinase 6 Enhances KAT2 Shaker Channel Activity in Arabidopsis thaliana

2021 ◽  
Vol 22 (4) ◽  
pp. 1596
Author(s):  
Elsa Ronzier ◽  
Claire Corratgé-Faillie ◽  
Frédéric Sanchez ◽  
Christian Brière ◽  
Tou Cheu Xiong
Keyword(s):  
Arabidopsis Thaliana ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Physical Interaction ◽  
Fluorescence Lifetime Imaging ◽  
Dependent Manner ◽  
In Planta ◽  
Knock Out ◽  
Calcium Dependent ◽  
Dependent Protein

Post-translational regulations of Shaker-like voltage-gated K+ channels were reported to be essential for rapid responses to environmental stresses in plants. In particular, it has been shown that calcium-dependent protein kinases (CPKs) regulate Shaker channels in plants. Here, the focus was on KAT2, a Shaker channel cloned in the model plant Arabidopsis thaliana, where is it expressed namely in the vascular tissues of leaves. After co-expression of KAT2 with AtCPK6 in Xenopuslaevis oocytes, voltage-clamp recordings demonstrated that AtCPK6 stimulates the activity of KAT2 in a calcium-dependent manner. A physical interaction between these two proteins has also been shown by Förster resonance energy transfer by fluorescence lifetime imaging (FRET-FLIM). Peptide array assays support that AtCPK6 phosphorylates KAT2 at several positions, also in a calcium-dependent manner. Finally, K+ fluorescence imaging in planta suggests that K+ distribution is impaired in kat2 knock-out mutant leaves. We propose that the AtCPK6/KAT2 couple plays a role in the homeostasis of K+ distribution in leaves.

scholarly journals A Unique GTP-Dependent Sporulation Sensor Histidine Kinase in Bacillus anthracis

2008 ◽  
Vol 191 (3) ◽  
pp. 687-692 ◽  
Author(s):  
Francesca Scaramozzino ◽  
Andrea White ◽  
Marta Perego ◽  
James A. Hoch
Keyword(s):  
Bacillus Anthracis ◽  
Histidine Kinase ◽  
Catalytic Domain ◽  
Coiled Coil ◽  
Reverse Reaction ◽  
Forward Reaction ◽  
Critical Signal ◽  
Sensor Histidine Kinase ◽  
Virulence Plasmids ◽  
Kinase Catalytic Domain

ABSTRACT The Bacillus anthracis BA2291 gene codes for a sensor histidine kinase involved in the induction of sporulation. Genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay. Evidence suggests that the sensor domains inhibit BA2291 by titrating its activating signal ligand. Studies with purified BA2291 revealed that this kinase is uniquely specific for GTP in the forward reaction and GDP in the reverse reaction. The G1 motif of BA2291 is highly modified from ATP-specific histidine kinases, and modeling this motif in the structure of the kinase catalytic domain suggested how guanine binds to the region. A mutation in the putative coiled-coil linker between the sensor domain and the catalytic domains was found to decrease the rate of the forward autophosphorylation reaction and not affect the reverse reaction from phosphorylated Spo0F. The results suggest that the activating ligand for BA2291 is a critical signal for sporulation and in a limited concentration in the cell. Decreasing the response to it either by slowing the forward reaction through mutation or by titration of the ligand by expressing the plasmid-encoded sensor domains switches BA2291 from an inducer to an inhibitor of the phosphorelay and sporulation.

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