Detailed Information on Publication Record
2009
Effects of magnesium binding and beryllofluoridation on a component of the cytokinin signaling pathway studied by nuclear magnetic resonance
TŘÍSKOVÁ, Olga, Blanka PEKÁROVÁ, Veronika MOTÁČKOVÁ, Lukáš ŽÍDEK, Vladimír SKLENÁŘ et. al.Basic information
Original name
Effects of magnesium binding and beryllofluoridation on a component of the cytokinin signaling pathway studied by nuclear magnetic resonance
Name in Czech
Účinek navázání Mg(2+) a BeF3 na část cytokininové dráhy studované pomocí nukleární magnetické rezonance
Name (in English)
Effects of magnesium binding and beryllofluoridation on a component of the cytokinin signaling pathway studied by nuclear magnetic resonance
Authors
TŘÍSKOVÁ, Olga, Blanka PEKÁROVÁ, Veronika MOTÁČKOVÁ, Lukáš ŽÍDEK, Vladimír SKLENÁŘ, Jaromír MAREK and Lubomír JANDA
Edition
2009
Other information
Type of outcome
Konferenční abstrakt
Confidentiality degree
není předmětem státního či obchodního tajemství
Organization unit
Faculty of Science
Změněno: 9/4/2010 15:19, RNDr. Lubomír Janda, Ph.D.
Abstract
V originále
Cytokinins are important regulators of intrinsic developmental programs leading to de- and re-differentiation of plant cells. The cytokinin signal transduction seems to be mediated via multistep phospohorylation, similar to the action of bacterial two-component signalling systems. A soluble receiver domain of CKI1 receptor histidine kinase of Arabidopsis thaliana has been investigated by nuclear magnetic resonance (NMR) in this study. The domain was expressed in E. coli and labeled with stable isotopes (13)C, (15)N. Resonance frequencies have been assigned using standard strategy and conformational changes were monitored by running 2D (1)H-(15)N HSQC spectra. Effect of Mg(2+) has been studied in a series of titration experiments and the most significantly affected residues were identified using secondary chemical shift mapping. Activation of the protein, which cannot be studied in real time due to a short life-time of the activated form with phosphorylated aspartate, was investigated in an artificial system with phosphate replaced by beryllofluoride. In both cases, the observed chemical shift changes were mapped on a recently solved X-ray structure of the non-phosphorylated protein. In addition to the structural studies, molecular motions were investigated by N-15 NMR relaxation experiments. Series of relaxation spectra were obtained for free, Mg(2+)-bound, and beryllofluorinated protein and interpreted in terms of the Lipari-Szabo model-free approach. The observed changes are discussed in context of the X-ray structure of the free protein.
Links
MSM0021622415, plan (intention) |
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