The Evaluation of Conserved Amino Acids that Influence Polysubstrate Specificity in the Multidrug Resistance Transporter, EmrE
Date
2014-08-21
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Abstract
The study of the molecular mechanism of substrate recognition/binding by multidrug resistance transporters has taken different approaches. I have utilized a PCR-driven site-directed mutagenesis analysis to alter conserved amino acid residues within the Escherichia coli small multidrug transporter, EmrE. The EmrE variants generated were further assessed for their resistance ability to 19 structurally different quaternary cationic compounds (QCC) using a high-throughput microtitre plate assay. The underlying hypothesis is that the mutation of conserved amino acids will alter the resistance profile of EmrE to structurally different QCC and identify the specificity of these residues to specific characteristic(s) of QCC. Based on 1,254 resistance profiles, the plasticity of EmrE binding pocket can be explained by the presence of conserved amino acid residues with different substrate preferences. The significance of studying EmrE is that it provides an excellent model for understanding the polysubstrate specificity on a molecular basis relatable to other major transporters.
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Genetics, Microbiology, Biochemistry
Citation
Saleh, M. (2014). The Evaluation of Conserved Amino Acids that Influence Polysubstrate Specificity in the Multidrug Resistance Transporter, EmrE (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/28135