Detailed Information on Publication Record
2011
Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.
PEKÁROVÁ, Blanka, Tomáš KLUMPLER, Olga TŘÍSKOVÁ, Jakub HORÁK, Séverine JANSEN et. al.Basic information
Original name
Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.
Authors
PEKÁROVÁ, Blanka (203 Czech Republic, belonging to the institution), Tomáš KLUMPLER (203 Czech Republic, belonging to the institution), Olga TŘÍSKOVÁ (203 Czech Republic, belonging to the institution), Jakub HORÁK (203 Czech Republic, belonging to the institution), Séverine JANSEN (250 France, belonging to the institution), Radka DOPITOVÁ (203 Czech Republic, belonging to the institution), Petra BORKOVCOVÁ (203 Czech Republic, belonging to the institution), Veronika PAPOUŠKOVÁ (203 Czech Republic, belonging to the institution), Eliška NEJEDLÁ (203 Czech Republic, belonging to the institution), Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution), Jaromír MAREK (203 Czech Republic, belonging to the institution), Lukáš ŽÍDEK (203 Czech Republic, belonging to the institution), Jan HEJÁTKO (203 Czech Republic, belonging to the institution) and Lubomír JANDA (203 Czech Republic, guarantor, belonging to the institution)
Edition
The Plant Journal, England, BLACKWELL PUBLISHING, 2011, 0960-7412
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
Genetics and molecular biology
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 6.160
RIV identification code
RIV/00216224:14740/11:00050106
Organization unit
Central European Institute of Technology
UT WoS
000294827700008
Keywords in English
multistep phosphorelay; receiver domain; CKI1; crystal structure; NMR spectroscopy; Arabidopsis thaliana
Tags
International impact, Reviewed
Změněno: 1/5/2012 01:49, doc. RNDr. Jaromír Marek, Ph.D.
Abstract
V originále
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.
Links
ED1.1.00/02.0068, research and development project |
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GAP305/11/0756, research and development project |
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GA521/09/1699, research and development project |
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GD204/08/H054, research and development project |
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LC06034, research and development project |
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MSM0021622413, plan (intention) |
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MSM0021622415, plan (intention) |
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MUNI/A/0928/2009, interní kód MU |
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205872, interní kód MU |
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228461, interní kód MU |
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