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Abstract Detail

Biotic and abiotic stress

McNeilly, Daryl [1], Stone, Sophia [1].

Characterizing Potential Targets of KEG.

A plants ability to adapt to environmental stress is crucial for its ability to grow and develop to maturity. E3 ligases are one of the ways plants are able to produce a coping response. An E3 ligase works to regulate protein levels by tagging specific proteins with ubiquitin molecules; how proteins are tagged determines their fate in the cell. A common outcome for tagged proteins is to be sent to the 26S proteasome for destruction. The targets of an E3 ligase include proteins involved in many aspects of plant growth, development, hormone signaling, pathogen resistance and tolerance of abiotic stresses. Keep on Going (KEG) is an E3 ligase that negatively regulates the actions of the hormone abscisic acid (ABA) during early seedling establishment. A search for other potential targets of KEG identified formate dehydrogenase (FDH), which has been previously characterized as a stress response protein. FDH converts formate into CO2, serving to alleviate any detrimental effects accumulated formate can have on the cell. We are interested in determining if FDH is ubiquitnated and degraded by the 26S proteasome and if KEG is responsible for the regulation of FDH. Preliminary results show that FDH is being modified and that KEG has the capability of attaching ubiquitin molecules to FDH. It has also been shown that FDH is being degraded by the 26S proteasome. In addition, Arabidopsis thaliana seedlings overexpressing KEG were found to be more sensitive to exogenous formate than their wild-type counter parts. These results suggest that FDH is regulated by KEG, indicating yet another possible role for KEG in regulating plant stress response.

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1 - Dalhousie University, Biology, 1355 Oxford Street PO BOX 15000, Halifax, NS, B3H 4R2, Canada

none specified

Presentation Type: Poster:Posters for Topics
Session: P
Location: Hall D/The Shaw Conference Centre
Date: Monday, July 27th, 2015
Time: 5:30 PM
Number: PBA007
Abstract ID:874
Candidate for Awards:CSPB President's Award for Best Student Presentation

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