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@inproceedings{911185,
author = {Pekárová, Blanka and Klumpler, Tomáš and Třísková, Olga and Horák, Jakub and Žídek, Lukáš and Marek, Jaromír and Dopitová, Radka and Hejátko, Jan and Janda, Lubomír},
address = {Suzhou, China},
edition = {1},
keywords = {vícekomponentní fosforylace, 3-D struktura, NMR analýza},
language = {eng},
location = {Suzhou, China},
pages = {47-47},
publisher = {Cold Spring Harbor Conferences Asia},
title = {The receiver domain of sensor histidine kinase of CKI1: its dynamic structure and binding specificity.},
url = {http://meetings.cshl.edu/CSHAsia/plants10.html},
year = {2010}
}
TY - JOUR
ID - 911185
AU - Pekárová, Blanka - Klumpler, Tomáš - Třísková, Olga - Horák, Jakub - Žídek, Lukáš - Marek, Jaromír - Dopitová, Radka - Hejátko, Jan - Janda, Lubomír
PY - 2010
TI - The receiver domain of sensor histidine kinase of CKI1: its dynamic structure and binding specificity.
PB - Cold Spring Harbor Conferences Asia
CY - Suzhou, China
KW - vícekomponentní fosforylace, 3-D struktura, NMR analýza
UR - http://meetings.cshl.edu/CSHAsia/plants10.html
N2 - In Arabidopsis multistep phosphorelay (MSP) signalling, the signal is transferred from sensor histidine kinase (HK) via histidine-containing phosphotransfer proteins (AHP1-5) to nuclear response regulators. In contrast to bacteria, MSP protein interactions in plants are supposed to be rather non-specific. Using both in vivo and in vitro assays we have found that the C-terminal receiver domain of HK CKI1 (CKI1RD) interacts with AHP2, 3 and 5 with different affinities. We determined crystal structure of free CKI1RD and CKI1RD in a complex with Mg2+. We have found that CKI1RD shares a particular similarity with the only known structure of plant HK, ETR1RD, with the main differences in the loop 3. Structural dynamics of CKIRD in solution was studied in detail by NMR in the absence or presence of Mg2+ that was shown to be indispensable to the transphosphorylation activity and BeF3-, the isomorphous stable phosphate analogue. Finally, using in vitro assay (indirect ELISA) we have found, that presence of Mg2+ and acetyl phosphate on one side and BeF3- on the other one affects the interaction of CKI1RD with its downstream signalling partners and may modulate AHP binding specificity in MSP signalling. Observed structural changes, their dynamics and potential influence on signal transduction specificity via MSP in plants will be discussed in detail.
ER -
PEKÁROVÁ, Blanka, Tomáš KLUMPLER, Olga TŘÍSKOVÁ, Jakub HORÁK, Lukáš ŽÍDEK, Jaromír MAREK, Radka DOPITOVÁ, Jan HEJÁTKO a Lubomír JANDA. \textit{The receiver domain of sensor histidine kinase of CKI1: its dynamic structure and binding specificity.}. 1. vyd. Suzhou, China: Cold Spring Harbor Conferences Asia, 2010, s.~47.
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