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Plants regulate cellular processes based on the presence or absence of light through a combination of anticipatory (circadian) and reactive (light responsive) mechanisms. Together, these mechanisms allow plants to dynamically adapt to their daily environment as well as signal developmental events (e.g. flowering). To date, the extent to which diurnal plant cell regulation is controlled by changes in protein abundance and/or post-translational protein modifications (PTMs) remains poorly understood.
PTMs are central to the proper functioning of eukaryotic cells. They represent fast-acting, fine-tuning mechanisms for regulating protein activities, changes in sub-cellular localization and protein-protein interactions, amongst others, collectively resulting in diverse biological outcomes. Protein phosphorylation and protein acetylation are two of the the most abundant PTMs identified to date. Given this, our work is focused on identifying and characterizing plant cell processes diurnally regulated by these PTMs. To do this, we employ quantitative proteomics to examine the model plant Arabidopsis thaliana from a systems perspective. Targets of interest are further investigated using a combination of molecular and cellular biology, biochemistry as well as targeted proteomics. |
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