Abstract

Nutrient sensing kinases sense available nutrients and regulate cell activity accordingly. Three of these enzymes are AMP regulated kinase (AMPK, or Snf1 in yeast), PAS kinase, and target of rapamycin (TOR), are conserved from yeast to man and have overlapping function. AMPK and Snf1 are important in sensing when nutrient status in the cell is low and down regulating energy consuming pathways. PAS kinase is required for glucose homeostasis in the cell, and responds to glucose levels. TOR senses nutrients such as amino acids and upregulates cell growth pathways primarily through protein synthesis. Due to the varying nature of these enzymes, cross talk is expected in order for the cell to properly regulate cellular metabolism and growth in response to energy and nutrient availability. Previous studies have shown that activation of yeast PAS kinase under nutrient stress conditions requires the presence of Snf1. The aim of this thesis is to determine whether Snf1 directly phosphorylates and activates PAS kinase through both in vivo and in vitro approaches. PAS kinase was found to require Snf1 for both activation and phosphorylation in vivo. In vitro kinase assays were also performed to confirm a direct phosphorylation event. The results from this study support the direct phosphorylation and activation of PAS kinase by Snf1, linking cellular energy status to glucose allocation.

Degree

MS

College and Department

Life Sciences; Microbiology and Molecular Biology

Rights

http://lib.byu.edu/about/copyright/

Date Submitted

2014-09-01

Document Type

Thesis

Handle

http://hdl.lib.byu.edu/1877/etd7295

Keywords

nutrient sensing kinases, target of rapamycin (TOR), AMP regulated kinase (AMPK), PAS kinase (PSK or PASK), Osh7, cellular metabolism

Included in

Microbiology Commons

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