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An investigation of the role of stress-responsive aldo-keto reductases in Arabidopsis thaliana

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dc.contributor.advisor Rothstein, Steven Lockhart, Morgan 2015-11-25T15:38:17Z 2015-11-25T15:38:17Z 2015-10 2015-10-30 2015-11-25
dc.description.abstract Aldo-keto reductases (AKRs) are a superfamily of enzymes which participate in redox reactions involving a wide range of carbonyl-containing substrates. Due to their lack of substrate specificity, AKRs may be involved in widespread toxicant metabolism, including the reduction of toxic methylglyoxal. Overexpression of OsMYB55 conferred heat-tolerance on rice and maize while maize lines demonstrated an over-accumulation of the metabolite 1,2-propanediol and increased expression of a number of AKRs. These findings point to a biochemical mechanism, linking heat tolerance with the production of 1,2-propanediol by one or more AKRs. This study demonstrates the heat-induced expression of three Arabidopsis AKRs. T2 generation overexpression lines resisted the negative effects of paraquat toxicity, a phenotype which correlates with the affinity of recombinantly-expressed proteins for the substrate methylglyoxal in vitro. Exogenous application of 1,2-propanediol demonstrated no protective effect but recommendations are made for a robust, high-throughput method for the quantification of endogenous 1,2-propanediol using HPAEC-PAD. en_US
dc.language.iso en en_US
dc.rights Attribution-NonCommercial-ShareAlike 2.5 Canada *
dc.rights.uri *
dc.subject aldo-keto reductase en_US
dc.subject Arabidopsis en_US
dc.subject abiotic stress en_US
dc.subject stress tolerance en_US
dc.subject methylglyoxal en_US
dc.subject 1,2-propanediol en_US
dc.subject AKR en_US
dc.title An investigation of the role of stress-responsive aldo-keto reductases in Arabidopsis thaliana en_US
dc.type Thesis en_US Molecular and Cellular Biology en_US Master of Science en_US Department of Molecular and Cellular Biology en_US
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Attribution-NonCommercial-ShareAlike 2.5 Canada Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 2.5 Canada