The minimal stress proteome contains proteins that are conserved in all organisms and have a central role in the environmental stress response. Because mechanisms of intracellular signaling have diverged grealty in the eukaryotic and prokaryotic lineages and cellular stress response networks have acquired increased complexity during evolution the minimal stress proteome only represents a small part of the overall stress proteome in most cells. Nevertheless, the minimal stress proteome represents an excellent starting point for unraveling the osmotic stress signaling network.

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We utilize a variety of reverse genetics, recombinant DNA, physiological, ecological, evolutionary genetics, and cytogenetic methods but emphasize an approach built around proteomics. Proteins are the main executioners of cell-, tissue-, and organ- function. Proteins are also the major nodes within the stress signaling networks. Thus, we are particularly focusing on multi-dimensional protein separation technology and MALDI-TOF-TOF mass spectrometry (MS/MS) based approaches. We also utilize laser scanning cytometry (LSC) based techniques for characterizing proteome modulation in response to environemtal stress. This technological focus on state-of-the art proteomics enables high throughput identification and in-depth characterization of critical elements in the osmotic stress response network.

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