2010
In vivo analysis of protein-protein interactions within the two-component signaling network in Arabidopsis.
HRDINOVÁ, Vendula; Jan HEJÁTKO a Jakub HORÁKZákladní údaje
Originální název
In vivo analysis of protein-protein interactions within the two-component signaling network in Arabidopsis.
Název česky
In vivo analýza protein-proteinových interakcí dvoukomponentní signální dráhy Arabidopsis
Autoři
HRDINOVÁ, Vendula; Jan HEJÁTKO ORCID a Jakub HORÁK
Vydání
XXIVth Genetic Days 2010, 2010
Další údaje
Jazyk
angličtina
Typ výsledku
Konferenční abstrakt
Obor
Genetika a molekulární biologie
Stát vydavatele
Česká republika
Utajení
není předmětem státního či obchodního tajemství
Označené pro přenos do RIV
Ne
Organizační jednotka
Přírodovědecká fakulta
ISBN
978-80-7375-423-5
Klíčová slova česky
Protein-proteinové interakce, Arabidopsis, Dvoukomponentní signaling
Klíčová slova anglicky
Protein-protein interaction, Arabidopsis, Two-component signaling
Štítky
Změněno: 8. 3. 2011 11:19, Mgr. Jakub Horák, Dr. rer. nat.
V originále
Two-component systems (TCS) belong to important sensing/response mechanisms in higher plants. This mechanism is used to perceive and transduce the signal of cytokinin and ethylene, plant hormones regulating variety of processes of growth and development. Function and composition of TCS have been intensively studied mostly in Arabidopsis thaliana. In this model plant TCS are composed of hybrid histidine kinases (AHKs, 8 genes), histidine-containting phosphotransfer proteins (AHPs, 6 genes) and response regulators (ARRs, 24 genes), that are biochemically linked by His-to-Asp phosphorelay. The specific interactions between AHPs and the receiver domains of AHKs could represent a potent mechanism how the specificity of cellular responses to different signals is achieved within the complex two-component signaling network.In this study the interactions between all receiver domains of AHKs and all six AHPs were analyzed in vivo. Using the modified MatchmakerTM yeast two-hybrid system (Clontech) were confirmed known and revealed novel interactions between these two families. As an independent method for the results verification was carried out Bimolecular Fluorescence Complementation analysis (BiFC) in transiently transformed tobacco leaves. Quantification of the fluorescence intensity in this analysis has also shown the differences between affinities of the AHPs to the receiver domains. We revealed that all receiver domains of AHKs interact with a specific set of AHPs. AHP5 interacts with each of the receiver domains, other AHPs interact more specifically. Receiver domains of AHK1, AHK5, CKI1 and ethylene receptors interact with the AHPs with higher affinity then the cytokinin receptors.
Česky
Cílem této práce bylo testovat interakce mezi receiverovými doménami Histidinkináz a AHP proteiny. Použitím metody kvasinkového dvouhybridního systému modifikovaný MatchmakerTM yeast two-hybrid system (Clontech)byly potvrzeny již známé a objeveny nové interakce mezi těmito rodinami proteinů. Jako nezávislá metoda pro potvrzení těchto interakcí byla použita Bimolekulární fluorescenční komplementace (BiFC)v transientně transformovaných listech tabáku (Nicotiana Benthamiana). Two-component systems (TCS) belong to important sensing/response mechanisms in higher plants. This mechanism is used to perceive and transduce the signal of cytokinin and ethylene, plant hormones regulating variety of processes of growth and development. Function and composition of TCS have been intensively studied mostly in Arabidopsis thaliana. In this model plant TCS are composed of hybrid histidine kinases (AHKs, 8 genes), histidine-containting phosphotransfer proteins (AHPs, 6 genes) and response regulators (ARRs, 24 genes), that are biochemically linked by His-to-Asp phosphorelay. The specific interactions between AHPs and the receiver domains of AHKs could represent a potent mechanism how the specificity of cellular responses to different signals is achieved within the complex two-component signaling network.
Návaznosti
| GD204/08/H054, projekt VaV |
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| LC06034, projekt VaV |
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