Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase from Arabidopsis thaliana

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F17%3A00095060" target="_blank" >RIV/00216224:14740/17:00095060 - isvavai.cz</a>

Result on the web

<a href="http://www.jbc.org/content/early/2017/08/31/jbc.M117.790212.short" target="_blank" >http://www.jbc.org/content/early/2017/08/31/jbc.M117.790212.short</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M117.790212" target="_blank" >10.1074/jbc.M117.790212</a>

Result language

angličtina

Original language name

Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase from Arabidopsis thaliana

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10600 - Biological sciences

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Volume of the periodical

292

Issue of the periodical within the volume

42

Country of publishing house

US - UNITED STATES

Number of pages

16

Pages from-to

17525-17540

UT code for WoS article

000414009300032

EID of the result in the Scopus database

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