Role of BMH proteins in the regulation of yeast enzyme neutral trehalase. The overall goal of this project is to understand the structural basis of BMH–dependent regulation of the activity of the enzyme Neutral trehalase (NTH1). Site-directed mutagenesis, steady-state fluorescence spectroscopy, time-resolved fluorescence spectroscopy, X-ray crystallography, analytical ultracentrifugation and enzyme kinetics measurements will be the principal tools. NTH1 is responsible for trehalose degradation and is required in a variety stress conditions. Activity of theNTH1 enzyme was just recently found to be mediated by BMH1 and BMH2 binding in yeast. The role of yeast BMH proteins in the regulation of NTH1 seems to increase the enzymatic activity of the NTH1 enzyme. However details concerning interaction between the BMH proteins and NTH1 remain still unknown. Since trehalose metabolism is an essential component of the stress response in yeast cells, thus, the elucidation of the mechanisms of NTH1 protein regulation, which is still unresolved, would provide us with important information concerning mechanisms of both the 14-3-3 protein function and the regulation of the neutral trehalase activity in yeast.
2005 RNDr. Biochemistry, Charles University, Prague, Faculty of Science
2005 PhD. Medicinal Biophysics, Charles University, Prague, 2st Faculty of Medicine
1995 MSc. Physical chemistry, Charles University, Prague, Faculty of Science
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