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Jay J. Thelen

Jay Thelen

Professor
Department of Biochemisty

E-mail: thelenj at missouri dot edu
Office address: 271g Bond Life Sciences Center
Office phone: 573-884-1325
Lab address: 204 Bond Life Sciences Center
Lab phone: 573-884-5979

Plant seeds are an important renewable source of biosynthetic polymers including protein, starch, oil and fiber. The amount of these biosynthates in harvested seed varies from negligible to a majority of total mass. Though the biosynthetic pathways for seed storage compounds are mostly known it is not clear how these pathways are regulated to produce higher quantities of oil versus starch or protein. With recent technological advances in the area of mass spectrometry in conjunction with maturing plant gene databases, high throughput identification of proteins from model and crop plants is technically feasible. Most of the ongoing research in my lab is centered on the development of quantitative proteomics approaches and applying these strategies towards seed filling in oilseeds, plants that accumulate oil as the primary storage reserve. We are using quantitative proteomics data to predict metabolic flow in diverse oilseeds such as castor, canola, soybean and sunflower with particular emphasis on carbon assimilation and intermediary metabolism. I am also interested in the regulation and biochemistry of de novo fatty acid synthesis and triacylglycerol accumulation in oilseeds.

arabidopsis developing seed protein

Global protein profiling of oilseeds using two-dimensional gel electrophoresis has revealed multiple isoforms for many metabolic activities. One reason for this could be post-translational modification, most notably protein phosphorylation. It is well known that rate-limiting or branch point enzymes are strategic points for 'fine' control of metabolism by reversible phosphorylation. To investigate this further, members of my lab are also systematically investigating phosphoprotein networks during seed-filling in model and crop oilseeds using advanced proteomics approaches and instrumentation. We using techniques such as Multistage Activation and Electron Transfer Dissociation on an LTQ-XL ETD mass spectrometer to map phosphorylation sites and AQUA peptides for quantification of phosphorylation flux dynamics in response to abiotic and biotic stimuli.

Specific Projects

  • Developing tools and strategies for comprehensive, quantitative analysis of plant proteomes
  • 2-DE analysis of seed filling in soybean, rapeseed, Arabidopsis, and castor
  • Quantitative characterization of phosphoproteins expressed during seed development using 2-DE and LC-MS/MS
  • Organellar proteomics comparing rapeseed leaf chloroplasts and developing embryo leucoplasts
  • Seed oil content protein biomarker discovery using breeding and transgenic germplasm

 

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