Publication details

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

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.
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