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

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 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.

Homology modelling of a sensor histidine kinase from Aeromonas hydrophila

2009 ◽  
Vol 16 (5) ◽  
pp. 1003-1009 ◽  
Author(s):  
Mobashar Hussain Urf Turabe Fazil ◽  
Sunil Kumar ◽  
Naidu Subbarao ◽  
Haushila Prasad Pandey ◽  
Durg Vijai Singh
Keyword(s):  
Aeromonas Hydrophila ◽  
Histidine Kinase ◽  
Homology Modelling ◽  
Sensor Histidine Kinase

scholarly journals Routes of phosphoryl group transfer during signal transmission and signal decay in the dimeric sensor histidine kinase ArcB

2018 ◽  
Vol 293 (34) ◽  
pp. 13214-13223 ◽  
Author(s):  
Juan L. Teran-Melo ◽  
Gabriela R. Peña-Sandoval ◽  
Hortencia Silva-Jimenez ◽  
Claudia Rodriguez ◽  
Adrián F. Alvarez ◽  
...  
Keyword(s):  
Histidine Kinase ◽  
Signal Transmission ◽  
Phosphoryl Group ◽  
Sensor Histidine Kinase ◽  
Group Transfer ◽  
Signal Decay

scholarly journals 1P-260 The Photoreaction of the PYP Domain in the Light Sensor Histidine Kinase Ppr is Influenced by the C-terminal Domains(The 46th Annual Meeting of the Biophysical Society of Japan)

2008 ◽  
Vol 48 (supplement) ◽  
pp. S62
Author(s):  
Hironari Kamikubo ◽  
Tomonori Koyama ◽  
Michihiro Hayashi ◽  
Kumiko Shirai ◽  
Yoichi Yamazaki ◽  
...  
Keyword(s):  
Annual Meeting ◽  
Histidine Kinase ◽  
Sensor Histidine Kinase ◽  
Light Sensor ◽  
Biophysical Society ◽  
Terminal Domains

scholarly journals Ethanolamine Activates a Sensor Histidine Kinase Regulating Its Utilization in Enterococcus faecalis

2008 ◽  
Vol 190 (21) ◽  
pp. 7147-7156 ◽  
Author(s):  
María Florencia Del Papa ◽  
Marta Perego
Keyword(s):  
Enterococcus Faecalis ◽  
Histidine Kinase ◽  
Intestinal Tract ◽  
Response Regulator ◽  
Synthetic Medium ◽  
Fold Increase ◽  
Ecological Niches ◽  
Bacterial Invasion ◽  
Sensor Histidine Kinase

ABSTRACT Enterococcus faecalis is a gram-positive commensal bacterium of the human intestinal tract. Its opportunistic pathogenicity has been enhanced by the acquisition of multiple antibiotic resistances, making the treatment of enterococcal infections an increasingly difficult problem. The extraordinary capacity of this organism to colonize and survive in a wide variety of ecological niches is attributable, at least in part, to signal transduction pathways mediated by two-component systems (TCS). Here, the ability of E. faecalis to utilize ethanolamine as the sole carbon source is shown to be dependent upon the RR-HK17 (EF1633-EF1632) TCS. Ethanolamine is an abundant compound in the human intestine, and thus, the ability of bacteria to utilize it as a source of carbon and nitrogen may provide an advantage for survival and colonization. Growth of E. faecalis in a synthetic medium with ethanolamine was abolished in the response regulator RR17 mutant strain. Transcription of the response regulator gene was induced by the presence of ethanolamine. Ethanolamine induced a 15-fold increase in the rate of autophosphorylation in vitro of the HK17 sensor histidine kinase, indicating that this is the ligand recognized by the sensor domain of the kinase. These results assign a role to the RR-HK17 TCS as coordinator of the enterococcal response to specific nutritional conditions existing at the site of bacterial invasion, the intestinal tract of an animal host.

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