Dynamic structure and binding specifity of the receiver domain of sensor histidine kinase CKI1

Warning

This publication doesn't include Faculty of Sports Studies. It includes Faculty of Science. Official publication website can be found on muni.cz.

Authors	PEKÁROVÁ Blanka KLUMPLER Tomáš TŘÍSKOVÁ Olga HORÁK Jakub ŽÍDEK Lukáš MAREK Jaromír DOPITOVÁ Radka HEJÁTKO Jan JANDA Lubomír
Year of publication	2010
Type	Article in Proceedings
MU Faculty or unit	Faculty of Science
Citation
Web	http://events.emagister.co.uk/conferences/20th_ipgsa_conference__international_plant_growth_substances_association/14212
Field	Biochemistry
Keywords	multistep phosphorelay, crystal structure, NMR analysis, CKI1
Description	In the Arabidopsis two-component signaling, the signal is transfered from sensor histidine kinase via histidine-containing phosphotransfer proteins (AHP1-5) to nuclear response regulators. Here we show the receiver domain of histidine kinase CYTOKININ-INDEPENDENT1 (CKI1RD) interacts in vivo and in vitro with AHP2, 3 and 5 with different affinities. To unravel the molecular determinants of observed specificity, we determined crystal structure of free CKI1RD and CKI1RD in complex with magnesium ions. Dynamics of CKI1RD solution structure has been studied in details by NMR in absence or presence of magnesium ions and beryllium fluoride.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Molecular basis of cell and tissue regulations Regulation of morphogenesis of plant cells and organs Immunomodulation as a functional proteomics tool for cytokinin signaling study in Arabidopsis thaliana