BIOCHEMISTRY AT MU
FACULTY RESEARCH
ACADEMICS
CONTACT LISTS
POSITION OPENINGS
| Email: | thelenj@missouri.edu |
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| Phone: | (573) 884-1325 | |
| Lab: | (573) 884-5979 | |
| Fax: | (573) 884-9676 | |
| Office: | 271G Bond Life Sciences Center | |
| Mailing Address: |
Biochemistry
271G Bond Life Sciences Center University of Missouri-Columbia Columbia, MO 65211 |
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| Research Areas: |
Proteomics and phosphoproteomics of seed development in oil seeds. |
Educational Background
| BS | 1994 | University of Nebraska | Lincoln, Neb. | Biochemistry |
| PhD | 1998 | University of Missouri | Columbia, Mo. | Molecular Biology/Biochemistry |
Research Description
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.
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.
Specific Projects
Research website: www.oilseedproteomics.missouri.edu
Selected Publications
Miernyk JA, Thelen JJ (2007) Biochemical approaches for discovering protein-protein interactions. Plant J. In press
Hajduch M, Casteel JE, Tang S, Hearne LB, Knapp S, Thelen JJ (2007) Proteomic analysis of near isogenic sunflower varieties differing in seed oil traits. J. Proteome Res. In press
Agrawal GK, Thelen JJ (2006) Large-scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape. Mol. Cell. Prot. 5:2044-2059
Kojima M, Casteel J, Miernyk JA, Thelen JJ (2006) The effects of down-regulating expression of Arabidopsis thaliana membrane-associated acyl-CoA binding protein 2 on acyl-lipid composition. Plant Science. 172:36-44
Katavic V, Agrawal GK, Hajduch M, Harris SL, Thelen JJ (2006) Protein and lipid composition analysis of oil bodies from two Brassica napus cultivars. Proteomics. 6: 4586-4598
Mooney BP, Miernyk JA, Greenlief CM, Thelen JJ (2006) Using quantitative proteomics of Arabidopsis roots and leaves to predict metabolic activity. Physiol. Plant. 128:237-250
Hajduch M, Casteel JE, Hurrelmeyer KE, Song Z, Agrawal GK, Thelen JJ (2006) Proteomic analysis of seed filling in Brassica napus: Developmental characterization of metabolic isozymes using high-resolution two-dimensional gel electrophoresis. Plant Physiol. 141:32-46
Employment Opportunities