| Cysteinyl t-RNA synthetase (CysRS), an enzyme that catalyzes the attachment of cysteine to its cognate tRNA, is an example of a protein with well characterized halophilic adaptations. Using the Halobacterium salinarum CysRS, we are investigating how the protein interacts with potassium, which seems to maintain its structure and stability. The effects of the metals on the protein were tested through equilibrium dialysis and atomic absorption spectroscopy (AAS). The goal was to determine the rate of diffusion over time and compare the results between the CysRS and E.coli CysRS, a negative control. It was observed that the halophilic protein binds to potassium faster than the nonhalophilic, E. coli protein. By characterizing this interaction, we estimated the binding constant of the protein, Kd, to the metal. The binding constant of the protein can contribute in designing techniques to be used in environmental remediation that could help us clean up metal contaminated sites.
Key Words: Halophile, Cysteinyl t-RNA synthetase, Halobacterium salinarum, Potassium. |