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Content archived on 2024-05-29

Dynamics of RAR1-SGT1 complexes in disease resistance

Objective

Genetic approaches has led to the identification of several components of the gene-for-gene resistance pathway. RAR1 and SGT1 are required for the function of many disese resistance R proteins. RAR1 and SGT1 interact with each other and with HSP90, a cytosolic chaperon also required for the function of some R proteins. SGT1 presents co-chaperone features and interaction between HSP90 and R-proteins has also been reported.
Collectively, these data suggest that RAR1 and SGT1 proteins might be components of R-protein heterocomplexes or be required for their formation or activation upon pathogen infection. Although RAR1, SGT1 and HSP90 interacts with each others, it remains to be shown whether RAR1 and/or SGT1 associate together with HSP90 and R proteins in a single complex. Additionally, SGT1 has been demonstrated to be associated with the SCF E3 ubiquitin ligase and COP9 signalosome complexes, suggesting that RAR1-SGT1 complexes may also play a role in the ubiquitin/proteasome system. In this project I assess the role of RAR1-SGT1 complexes in R-protein signalling.
The project will adopt a biochemical approach to reconstitute R proteins and the RAR1-SGT1-HSP90 complexes in vitro and to identify further components of the RAR1-SGT1 hetero-complexes from plant extr acts using affinity chromatography methods followed by mass spectrometry. I also aim to identify new RAR1 and SGT1 interacting proteins using a split-ubiquitin yeast two hybrid screening. In addition, I plan to visualise these interactions in vivo using Bi FC analysis to study their dynamics during the defence response.

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Call for proposal

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FP6-2004-MOBILITY-5
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Funding Scheme

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EIF - Marie Curie actions-Intra-European Fellowships

Coordinator

SAINSBURY LABORATORY
EU contribution
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Total cost

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