The Traaseth Group published a study entitled, "Inducing conformational preference of the membrane protein transporter EmrE through conservative mutations" in eLife. NYU Research highlighted the study, noting that "swapping a single amino acid in a simple bacterial protein changes its structure and function, revealing the effects of complex gene evolution. The study—conducted using E. coli bacteria—can help researchers to better understand the evolution of transporter proteins and their role in drug resistance." The authors of the work are postdoctoral fellow Maureen Leninger, graduate student Ampon Sae Her and Associate Professor of Chemistry Nate Traaseth.
To read the eLife article, click here.
To read the NYU Research Highlight article, click here.
Abstract: Transporters from bacteria to humans contain inverted repeat domains thought to arise evolutionarily from the fusion of smaller membrane protein genes. Association between these domains forms the functional unit that enables transporters to adopt distinct conformations necessary for function. The small multidrug resistance (SMR) family provides an ideal system to explore the role of mutations in altering conformational preference since transporters from this family consist of antiparallel dimers that resemble the inverted repeats present in larger transporters. Here, we show using NMR spectroscopy how a single conservative mutation introduced into an SMR dimer is sufficient to change the resting conformation and function in bacteria. These results underscore the dynamic energy landscape for transporters and demonstrate how conservative mutations can influence structure and function.
The research was supported by the National Institutes of Health and National Science Foundation.