
E-mail:thelenj@missouri.edu
Office: 271G Bond Life Sciences Center
Mail: Christopher S. Bond Life Sciences Center
271G Bond Life Sciences Center
University of Missouri
Columbia, MO 65211
Phone: 573-884-1325
Fax: 573-884-9676
Lab: 573-884-5979
| Degree | School | Location | Major |
| BS | University of Nebraska | Lincoln, Neb. | Biochemistry |
| PhD | University of Missouri | Columbia, Mo. | Molecular Biology/Biochemistry |
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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.
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 the 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.
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 use 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.
Chen M, Thelen JJ. ACYL-LIPID DESATURASE2 Is Required for Chilling and Freezing Tolerance in Arabidopsis. Plant Cell. 2013 Apr 12.
Havelund JF, Thelen JJ, Møller IM. Biochemistry, proteomics, and phosphoproteomics of plant mitochondria from non-photosynthetic cells. Front Plant Sci. 2013;4:51. doi: 10.3389/fpls.2013.00051. Epub 2013 Mar 13.
Gasulla F, Jain R, Barreno E, Guéra A, Balbuena TS, Thelen JJ, Oliver MJ. The response of Asterochloris erici (Ahmadjian) Skaloud et Peksa to desiccation: a proteomic approach. Plant Cell Environ. 2013 Jan 11. doi: 10.1111/pce.12065.
Ahsan N, Huang Y, Tovar-Mendez A, Swatek KN, Zhang J, Miernyk JA, Xu D, Thelen JJ. A versatile mass spectrometry-based method to both identify kinase client-relationships and characterize signaling network topology. J Proteome Res. 2013 Feb 1;12(2):937-48. doi: 10.1021/pr3009995. Epub 2013 Jan 15.
Yao Q, Bollinger C, Gao J, Xu D, Thelen JJ. P(3)DB: An Integrated Database for Plant Protein Phosphorylation. Front Plant Sci. 2012;3:206. doi: 10.3389/fpls.2012.00206. Epub 2012 Sep 7.
Postdoctoral opportunities
Research areas: Proteomics and phosphoproteomics of seed development and metabolism in oilseeds.
How to apply:
Electronic submission is encouraged, e-mail to thelenj@missouri.edu
Applicants should send CV and names of two references to:
Dr. Jay J. Thelen
Christopher S. Bond Life Sciences Center
271G Bond Life Sciences Center
University of Missouri
Columbia, MO 65211