Interactions of the receiver domain in histidine kinase receptors with the AHP proteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F09%3A00029998" target="_blank" >RIV/00216224:14310/09:00029998 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Interactions of the receiver domain in histidine kinase receptors with the AHP proteins

Popis výsledku v původním jazyce

Two-component systems belong to important sensing / response mechanisms in higher plants. AHP proteins interact with histidine kinase receptors as well as with response regulators, and therefore link the signal recognition by membrane sensors with regulation of transcription via nuclear-located transcription factors that mediate plant responses to the environmental stimuli. In our study the interactions of CKI1 receiver domain with all six AHP proteins were analyzed in vivo. Using the yeast two-hybrid system we revealed that CKI1 receiver domain interacts with AHP2, AHP3 and AHP5, but not with AHP1, AHP4 and AHP6. In addition, bimolecular fluorescence complementation analysis (BiFC) was carried out in transiently transformed tobacco leaves and the interaction pattern was confirmed. Combining these two methods for analysis of protein-protein interactions in vivo we gained a rapid insight into the specificity of elements involved in a signalling cascade downstream of CKI1

Název v anglickém jazyce

Interactions of the receiver domain in histidine kinase receptors with the AHP proteins

Popis výsledku anglicky

Two-component systems belong to important sensing / response mechanisms in higher plants. AHP proteins interact with histidine kinase receptors as well as with response regulators, and therefore link the signal recognition by membrane sensors with regulation of transcription via nuclear-located transcription factors that mediate plant responses to the environmental stimuli. In our study the interactions of CKI1 receiver domain with all six AHP proteins were analyzed in vivo. Using the yeast two-hybrid system we revealed that CKI1 receiver domain interacts with AHP2, AHP3 and AHP5, but not with AHP1, AHP4 and AHP6. In addition, bimolecular fluorescence complementation analysis (BiFC) was carried out in transiently transformed tobacco leaves and the interaction pattern was confirmed. Combining these two methods for analysis of protein-protein interactions in vivo we gained a rapid insight into the specificity of elements involved in a signalling cascade downstream of CKI1

Druh

O - Ostatní výsledky

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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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)

Rok uplatnění

2009

Kód důvěrnosti údajů

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