Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F11%3A00050106" target="_blank" >RIV/00216224:14740/11:00050106 - isvavai.cz</a>

Výsledek na webu

<a href="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" target="_blank" >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</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/j.1365-313X.2011.04637.x" target="_blank" >10.1111/j.1365-313X.2011.04637.x</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.

Popis výsledku v původním jazyce

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 responseregulators. 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 ofCKI1 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 insolution, 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

Název v anglickém jazyce

Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.

Popis výsledku anglicky

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 responseregulators. 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 ofCKI1 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 insolution, 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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

The Plant Journal

ISSN

0960-7412

e-ISSN

—

Svazek periodika

67

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

13

Strana od-do

827-839

Kód UT WoS článku

000294827700008

EID výsledku v databázi Scopus

—