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Show UNDERGRADUATE RESEARCH ABSTRACTS SPRING 2007 Jared Rutter 59 Biochemistry of PAS Kinase Regulation Hana Sabic, (Jared Rutter) Department of Biochemistry University of Utah Metabolic processes are known to be controlled by various cellular signaling pathways. PAS kinase is a sensory enzyme that regulates metabolism through protein phosphorylation. We have found that there are two pathways that activate PAS kinase in S. cerevisiae: one is nutrient dependent (relies on carbon source) and the other is dependent on cell integrity stress. Remarkably, PAS kinase purified from yeast grown under activating conditions remains activated. The main goal of our research is to uncover mechanisms by which PAS kinase becomes activated. Since mammalian PAS kinase was found to play a role in obesity and diabetes, understanding of such mechanisms may lead to possible solutions to the pathogenesis of these conditions.! The focus of our research is to identify activating factors, such as protein modification, associated proteins or small molecule activators that are responsible for promoting the activation of the protein in vivo. To identify possible activating factors, TAP tag purification procedure was performed followed by analyzing the samples on a silver-stained 8% SDS PAGE gel. Silver-stained gel showed a band of PAS kinase size present in both untagged (control) and tagged raffinose fractions, suggesting a need for higher PAS kinase expression levels. This finding is consistent with the low expression levels known for this enzyme. 1 G.A. daSilvaXavier, J. Rutter, G. A. Rutter Involvement of PAS kinase in the stimulation of preproinsulin and pancreatic duodenum homeobox-1 gene expression by glucose. Proc. Natl. Acad. Sci. USA, 101:8319, 2004. |
