NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins

Warning

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

PEKÁROVÁ Blanka TŘÍSKOVÁ Olga ŽÍDEK Lukáš MAREK Jaromír HORÁK Jakub DOPITOVÁ Radka HEJÁTKO Jan JANDA Lubomír

Year of publication 2009
Type Conference abstract
MU Faculty or unit

Faculty of Science

Citation
Description In a multistep phosphorelay, the C-terminal receiver domain of sensor histidine kinases is supposed to be involved in protein-protein interactions with its downstream signalling partners, the AHP proteins. Here we show that CKI1RD interacts in vivo and in vitro with AHP2, 3, and 5 with different affinities. To understand protein-protein interactions on the molecular level, the structure of CKI1RD in solution has been studied in details by nuclear magnetic resonance (NMR). Effects of magnesium ions (Mg2+) and phosphate analogue beryllium fluoride on chemical shift changes of CKI1RD have been studied in a series of titration experiments and the most significantly affected residues were identified. Observed chemical shift changes were mapped on a solved crystallographic structure of the protein. Molecular motions were investigated by NMR relaxation experiments with free, Mg2+-bound, and beryllofluorinated CKI1RD. Based on these data and in combination with bioinformatics approach, we determined four regions that might be responsible for the observed specificity of protein-protein interactions between CKI1RD and individual AHP proteins.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.