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Virginia Commonwealth University

1. Uzzell, Jamar. STRUCTURAL BASIS FOR THERMAL STABILITY OF THERMOPHILIC TRMD PROTEINS.

Degree: MS, Biochemistry, 2011, Virginia Commonwealth University

Thermal stability of theG37 tRNA methyltransferase proteins from Thermotoga maritima and Aquifex aeolicus have been compared using Differential Scanning Calorimetry. It was shown that the Thermotoga protein is remarkably stable and is denatured at temperatures in excess of 100 degrees Centigrade. The Aquifex aeolicus protein was less stable, denaturing broadly at temperatures between 55 °C and 100 °C. In contrast, the mesophilic E. coli protein was completely denatured at 55 °C. Enzymatic activity of the proteins was measured at various temperatures. Both the Thermotoga and Aquifex enzymes are active at ambient temperatures, and display a significant decrease in activity when the temperature is raised above 50 °C. This may relate to subtle changes in protein structure causing an effect on the tRNA based assay. Both enzymes contain inter subunit disulfide bonds which might contribute to thermal stability. Assays of the enzymes in the presence of high concentrations of Dithiothreitol (DTT) did not significantly reduce activity at higher temperatures, but did stimulate activity at lower temperatures. Site directed mutagenesis of non -conserved protein sequences within Thermotoga maritima were initiated in order to determine what structures might confer heat stability on the protein. Alanine mutagenesis of lysine residues 103,104 led to reduced catalytic activity, but did increased activity at higher temperatures. Aspartate is the most common residue at the relative position 166 in the variable loop of most TrmD genes. It has been shown that in E. coli this is essential for catalytic activity and possibly the residue which carries out N1 deprotonation on residue G37 in tRNA. In Thermotoga glutamate is present at this position. Alanine mutagenesis of this residue did not eliminate activity suggesting another nearby residue may function in this capacity in the Thermotoga TrmD protein. Advisors/Committee Members: Walter M. Holmes.

Subjects/Keywords: TrmD; Thermophilies; Thermophilic; Aquifex aeolicus; Thermotoga maritima; DSC; Differential Scanning Calorimetry; Biochemistry, Biophysics, and Structural Biology; Life Sciences

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Uzzell, J. (2011). STRUCTURAL BASIS FOR THERMAL STABILITY OF THERMOPHILIC TRMD PROTEINS. (Thesis). Virginia Commonwealth University. Retrieved from https://doi.org/10.25772/6DKP-1H28 ; https://scholarscompass.vcu.edu/etd/2539

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Uzzell, Jamar. “STRUCTURAL BASIS FOR THERMAL STABILITY OF THERMOPHILIC TRMD PROTEINS.” 2011. Thesis, Virginia Commonwealth University. Accessed January 25, 2021. https://doi.org/10.25772/6DKP-1H28 ; https://scholarscompass.vcu.edu/etd/2539.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Uzzell, Jamar. “STRUCTURAL BASIS FOR THERMAL STABILITY OF THERMOPHILIC TRMD PROTEINS.” 2011. Web. 25 Jan 2021.

Vancouver:

Uzzell J. STRUCTURAL BASIS FOR THERMAL STABILITY OF THERMOPHILIC TRMD PROTEINS. [Internet] [Thesis]. Virginia Commonwealth University; 2011. [cited 2021 Jan 25]. Available from: https://doi.org/10.25772/6DKP-1H28 ; https://scholarscompass.vcu.edu/etd/2539.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Uzzell J. STRUCTURAL BASIS FOR THERMAL STABILITY OF THERMOPHILIC TRMD PROTEINS. [Thesis]. Virginia Commonwealth University; 2011. Available from: https://doi.org/10.25772/6DKP-1H28 ; https://scholarscompass.vcu.edu/etd/2539

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

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