Translational Frameshifting, which occurs during protein synthesis, is programmed by the mRNA sequence and also affected by the secondary mRNA structure. In our previous studies, multiple frameshifting steps were observed on a GA<sub>7</sub>G slippery mRNA without the downstream secondary structure. Although, high-yield “-1” and “-2” frameshiftings were detected, the strength of the internal mechanical force remains unknown. Previous mechanical force measurements from our lab indicate that elongation factor G binding and GTP hydrolysis are indispensable to multiple frameshifting steps. Recent characterization of structurally modified EF-G demonstrated that a reduced power stroke only lowered the percentage of translocation but did not introduce translocation error. Following this observation, power stroke on the slippery sites may indicate a reduced mechanical force strength due to a weaker force transmission from the tRNA to the mRNA, compared to normal translocation.<br/>To detect the power stroke of EF-G during frameshifting, force-induced remnant magnetization spectroscopy (FIRMS) with internal force references, will be used to precisely determine the force generated by EF-G in the process of ribosome translocation. Our force measurement detections indicate that the conformational restriction of EF-G lead to reduced mechanical force, therefore limited ribosomal translocation. This will help us determine the role of mechanical force during translational frameshifting. Further, these results could contribute to elucidating the inhibition mechanism of antibiotics such as Fusidic acid.

Modulation of EF-G power stroke during ribosomal frameshifting

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.