OTRUSINOVÁ, Olga, Gabriel DEMO, Petr PADRTA, Zuzana JASEŇÁKOVÁ, Blanka PEKÁROVÁ, Zuzana GELOVÁ, Agnieszka SZMITKOWSKA, Pavel KADEŘÁVEK, Séverine JANSEN, Milan ZACHRDLA, Tomáš KLUMPLER, Jaromír MAREK, Jozef HRITZ, Lubomír JANDA, Hideo IWAI, Michaela WIMMEROVÁ, Jan HEJÁTKO and Lukáš ŽÍDEK. Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase from Arabidopsis thaliana. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., vol. 292, No 42, p. 17525-17540. ISSN 0021-9258. doi:10.1074/jbc.M117.790212. 2017.
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Basic information
Original name Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase from Arabidopsis thaliana
Authors OTRUSINOVÁ, Olga (203 Czech Republic, belonging to the institution), Gabriel DEMO (703 Slovakia, belonging to the institution), Petr PADRTA (203 Czech Republic, belonging to the institution), Zuzana JASEŇÁKOVÁ (703 Slovakia, belonging to the institution), Blanka PEKÁROVÁ (203 Czech Republic, belonging to the institution), Zuzana GELOVÁ (203 Czech Republic, belonging to the institution), Agnieszka SZMITKOWSKA (616 Poland, belonging to the institution), Pavel KADEŘÁVEK (203 Czech Republic, belonging to the institution), Séverine JANSEN (250 France, belonging to the institution), Milan ZACHRDLA (203 Czech Republic, belonging to the institution), Tomáš KLUMPLER (203 Czech Republic, belonging to the institution), Jaromír MAREK (203 Czech Republic, belonging to the institution), Jozef HRITZ (703 Slovakia, belonging to the institution), Lubomír JANDA (203 Czech Republic, belonging to the institution), Hideo IWAI (246 Finland), Michaela WIMMEROVÁ (203 Czech Republic, belonging to the institution), Jan HEJÁTKO (203 Czech Republic, belonging to the institution) and Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution).
Edition Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 2017, 0021-9258.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 4.011
RIV identification code RIV/00216224:14740/17:00095060
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1074/jbc.M117.790212
UT WoS 000414009300032
Keywords in English histidine kinase; nuclear magnetic resonance (NMR); protein dynamic; protein phosphorylation; X-ray crystallography; receiver domain; relaxation dispersion
Tags CF NMR, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 12/4/2018 11:22.
Abstract
Multistep phosphorelay (MSP) cascades mediate responses to a wide spectrum of stimuli, including plant hormonal signaling, but several aspects of MSP await elucidation. Here, we provide first insight into the key step of MSP- mediated phosphotransfer in a eukaryotic system, the phosphorylation of the receiver domain of the histidine kinase CYTOKININ-INDEPENDENT 1 (CKI1(RD)) from Arabidopsis thaliana. We observed that the crystal structures of free, Mg2+-bound, and beryllofluoridated CKI1(RD) (a stable analogue of the labile phosphorylated form) were identical and similar to the active state of receiver domains of bacterial response regulators. However, the three CKI1(RD) variants exhibited different conformational dynamics in solution. NMR studies revealed that Mg2+ binding and beryllofluoridation alter the conformational equilibrium of the beta 3-beta 3 loop close to the phosphorylation site. Mutations that perturbed the conformational behavior of the beta 3-beta 3 loop while keeping the active- site aspartate intact resulted in suppression of CKI1 function. Mechanistically, homology modeling indicated that the beta 3 beta 3 loop directly interacts with the ATP- binding site of the CKI1 histidine kinase domain. The functional relevance of the conformational dynamics observed in the beta 3-beta 3 loop of CKI1(RD) was supported by a comparison with another A. thaliana histidine kinase, ETR1. In contrast to the highly dynamic beta 3- beta 3 loop of CKI1(RD), the corresponding loop of the ETR1 receiver domain (ETR1(RD)) exhibited little conformational exchange and adopted a different orientation in crystals. Biochem-ical data indicated that ETR1(RD) is involved in phosphorylation-independent signaling, implying a direct link between conformational behavior and the ability of eukaryotic receiver domains to participate in MSP.
Links
GA13-25280S, research and development projectName: Elucidating molecular mechanisms of cytokinins-ethylene crosstalk in the plant development
Investor: Czech Science Foundation
LM2015043, research and development projectName: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)
Investor: Ministry of Education, Youth and Sports of the CR
LQ1601, research and development projectName: CEITEC 2020 (Acronym: CEITEC2020)
Investor: Ministry of Education, Youth and Sports of the CR
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