The ribosome is the important complex molecular machine that is responsible for the correct translation of mRNA into protein. The ribosome is associated with various protein factors, including the GTPase Elongation Factor G (EF-G), which is responsible for catalyzing tRNA and mRNA translocation on the ribosome. EF-G has recently been shown to undergo a large conformational change between the pre-translocation state and post-translocation state, which implies force generation. However, the mechanism of translocation is still not fully understood. In order to understand the role of the force produced by EF-G in translocation fidelity, we will measure the force of various EF-G double-cysteine mutants. Using Force-Induced Remnant Magnetization Spectroscopy (FIRMS), developed by our lab, we are able to measure the force EF-G produces on the ribosome with 2-3 pN resolution, while also eliminating background. New mutation pairs situated in the Fusidic Acid binding pocket of EF-G have been produced in order to continue studying the role EF-G plays in translocation fidelity, as well as EF-G’s role in Fusidic acid resistance development. These pairs are focused on studying Fusidic acid resistance through single amino acid changes to residues thought to play important roles in Fusidic acid binding. Various mutations are done in order to fully understand the dynamics of this binding pocket.

Measuring the mechanical forces of Elongation Factor G mediated translocation

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.