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@article{956151,
author = {Pekárová, Blanka and Klumpler, Tomáš and Třísková, Olga and Horák, Jakub and Jansen, Séverine and Dopitová, Radka and Borkovcová, Petra and Papoušková, Veronika and Nejedlá, Eliška and Sklenář, Vladimír and Marek, Jaromír and Žídek, Lukáš and Hejátko, Jan and Janda, Lubomír},
article_location = {England},
article_number = {5},
doi = {http://dx.doi.org/10.1111/j.1365-313X.2011.04637.x},
keywords = {multistep phosphorelay; receiver domain; CKI1; crystal structure; NMR spectroscopy; Arabidopsis thaliana},
language = {eng},
issn = {0960-7412},
journal = {The Plant Journal},
title = {Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.},
url = {http://onlinelibrary.wiley.com/doi/10.1111/j.1365-313X.2011.04637.x/abstract;jsessionid=B5B70BA3083D8EC46EA118AB8CD89B26.d03t02?systemMessage=Wiley+Online+Library+will+be+disrupted+5+Nov+from+10-12+GMT+for+monthly+maintenance},
volume = {67},
year = {2011}
}
TY - JOUR
ID - 956151
AU - Pekárová, Blanka - Klumpler, Tomáš - Třísková, Olga - Horák, Jakub - Jansen, Séverine - Dopitová, Radka - Borkovcová, Petra - Papoušková, Veronika - Nejedlá, Eliška - Sklenář, Vladimír - Marek, Jaromír - Žídek, Lukáš - Hejátko, Jan - Janda, Lubomír
PY - 2011
TI - Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.
JF - The Plant Journal
VL - 67
IS - 5
SP - 827-839
EP - 827-839
PB - BLACKWELL PUBLISHING
SN - 09607412
KW - multistep phosphorelay
KW - receiver domain
KW - CKI1
KW - crystal structure
KW - NMR spectroscopy
KW - Arabidopsis thaliana
UR - http://onlinelibrary.wiley.com/doi/10.1111/j.1365-313X.2011.04637.x/abstract;jsessionid=B5B70BA3083D8EC46EA118AB8CD89B26.d03t02?systemMessage=Wiley+Online+Library+will+be+disrupted+5+Nov+from+10-12+GMT+for+monthly+maintenance
L2 - http://onlinelibrary.wiley.com/doi/10.1111/j.1365-313X.2011.04637.x/abstract;jsessionid=B5B70BA3083D8EC46EA118AB8CD89B26.d03t02?systemMessage=Wiley+Online+Library+will+be+disrupted+5+Nov+from+10-12+GMT+for+monthly+maintenance
N2 - Multistep phosphorelay (MSP) signaling mediates responses to a variety of important stimuli in plants. In Arabidopsis MSP, the signal is transferred from sensor histidine kinase (HK) via histidine phosphotransfer proteins (AHP1–AHP5) to nuclear response regulators. In contrast to ancestral two-component signaling in bacteria, protein interactions in plant MSP are supposed to be rather nonspecific. Here, we show that the C-terminal receiver domain of HK CKI1 (CKI1RD) is responsible for the recognition of CKI1 downstream signaling partners, and specifically interacts with AHP2, AHP3 and AHP5 with different affinities. We studied the effects of Mg2+, the co-factor necessary for signal transduction via MSP, and phosphorylation-mimicking BeF3 ) on CKI1RD in solution, and determined the crystal structure of free CKI1RD and CKI1RD in a complex with Mg2+. We found that the structure of CKI1RD shares similarities with the only known structure of plant HK, ETR1RD, with the main differences being in loop L3.
ER -
PEKÁROVÁ, Blanka, Tomáš KLUMPLER, Olga TŘÍSKOVÁ, Jakub HORÁK, Séverine JANSEN, Radka DOPITOVÁ, Petra BORKOVCOVÁ, Veronika PAPOUŠKOVÁ, Eliška NEJEDLÁ, Vladimír SKLENÁŘ, Jaromír MAREK, Lukáš ŽÍDEK, Jan HEJÁTKO a Lubomír JANDA. Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana. \textit{The Plant Journal}. England: BLACKWELL PUBLISHING, 2011, roč.~67, č.~5, s.~827-839. ISSN~0960-7412. Dostupné z: https://dx.doi.org/10.1111/j.1365-313X.2011.04637.x.
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