Jan A. Miernyk

Adjunct Professor of Biochemistry

Email:	miernykj@missouri.edu
Phone:	(573) 882-8167
Fax:	(573) 884-7850
Office:	102 Curtis Hall
Mailing Address:	Plant Genetics Research Unit 204 Curtis Hall University of Missouri-Columbia Columbia, MO 65211
Research Areas:	Protein targeting and folding in plants, organelle biogenesis, posttranslational modifications.

Educational Background

Notable Honors and Service

Research Description

Systems biology is a relatively recent term, and can be considered as an amalgam of "functional-omics" data and computational biology. While primarily descriptive as the system is developed, it then evolves to predictive as the system is increasingly defined. The ultimate goal is an integrative model that approaches the in silico organism.

A major focus of systems research in the Miernyk lab is soybean seed development. A descriptive platform has been developed that encompasses eight stages, and defines the periods of cell division/tissue differentiation, cellular specialization, lipid accumulation, protein accumulation, and preparation for quiescence. Total proteins were isolated from each stage and compared by Difference Gel Electrophoresis (DIGE). The patterns of change in protein abundance were analyzed by a combination of model-building, cluster analysis, and multidimensional scaling. Systems cartography is being used to describe the relationships among protein function, expression, localization, and biological interaction. The cartograph is constantly evolving, in all dimensions, as additional data are included.

Figure Legend: Analysis of soybean seed proteins by Difference Gel Electrophoresis (DIGE) to identify targets for further analysis.
The image is a comparison of proteins from stage S2 (labeled with CyDye3; Amersham) versus stage S3 (CyDye5-labeled). When the gels are imaged, spots that are relatively similar in protein abundance appear yellow, spots where protein abundance is increased in the second sample appear green, and those where protein abundance decreased appear red. Similar pairwise comparisons were made throughout seed development. Selected spots were subjected to in gel tryptic digestion, and peptide mass fingerprint analysis by MALDI-TOF mass spectrometry. Panel A, S2 v. S3; B, S3 v. S4; C, S4 v. S5; etc. The positions of marker protein migration are indicated to the left of the Y-axes; an estimate of the pI is indicated below the X-axes. The glycinin storage proteins are boxed in panel C.

Selected Publications

Miernyk JA, Johnston ML (2006) Chemical cross-linking immobilized-concanavalin A for use in proteomic analyses. Preparative Biochemistry and Biotechnology 36: 203-213

Mooney BP, Miernyk JA, Greenlief MC, Thelen JJ (2006) Using quantitative proteomics to predict metabolic activity. Physiologia Plantarum 128: 237-250

Kojima M, Casteel J, Miernyk JA, Thelen JJ (2007) 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

Miernyk JA, Szurmak B, Tovar-Mendez A, Randall DD, Muszynska G (2007) Is there a signal transduction pathway that links events at the plasma membrane to the phosphorylation state of the mitochondrial pyruvate dehydrogenase complex? Physiologia Plantarum 129: 104-113

Antoine W, Miernyk JA (2007) Shape-to-string mapping: A novel approach to clustering time-index biomics data. Online Journal of Bioinformatics 8: 139-153

Miernyk JA, Thelen JJ (2008) Biochemical approaches for discovering protein:protein interactions. Plant Journal in press