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DOE OSTI · 2589348

Frameshifting Stimulatory Sequence Induces Large Structural Change of Ribosomal Proteins When Bound to E. coli Ribosomes

Armbruster, Emily [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States); Univ. of Missouri, Columbia, MO (United States)]·Weiss, Kevin L. [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0000000264868007)·Petridis, Loukas [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)]·Borreguero Calvo, Jose [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)]·Byrnes, James [Brookhaven National Laboratory (BNL), Upton, NY (United States). National Synchrotron Light Source II (NSLS-II)]·Williams, Alexis N. [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Center for Nanophase Materials Sciences (CNMS)]·Cornish, Peter [Univ. of Missouri, Columbia, MO (United States)] (ORCID:0000000305740748)·Pingali, Sai Venkatesh [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0000000179614176)
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Abstract

Biological macromolecular machines occupy a continuum of structural conformations to perform cellular tasks. Mapping this conformational space provides an insight into its functionality. While the cryo-electron microscopy resolution revolution has expanded our ability to characterize the conformational continuums, there are obstacles in structurally characterizing regions of high flexibility. These technical barriers have impeded characterization of flexible ribosomal proteins when the ribosome is interacting with mRNA stem-loop structures such as a frameshifting stimulatory sequence (FSS). Small-angle neutron/X-ray scattering and electron microscopy were used to study ribosomal samples and compared structural differences between a ribosome that is bound to an FSS stem-loop compared to a ribosome bound to linear mRNA. This comparison shows that a large protein stalk elongates by 22% when the 70S interacts with an mRNA stem-loop. Finally, our results suggest that ribosomal proteins have extensive flexibility and may influence important ribosomal mechanisms, such as those that involve FSS.

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36 MATERIALS SCIENCEbacteriamonomersscatteringtheoretical modelsx-ray scattering

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Armbruster, Emily [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States); Univ. of Missouri, Columbia, MO (United States)], Weiss, Kevin L. [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0000000264868007), Petridis, Loukas [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)], Borreguero Calvo, Jose [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)], Byrnes, James [Brookhaven National Laboratory (BNL), Upton, NY (United States). National Synchrotron Light Source II (NSLS-II)], Williams, Alexis N. [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Center for Nanophase Materials Sciences (CNMS)], Cornish, Peter [Univ. of Missouri, Columbia, MO (United States)] (ORCID:0000000305740748), Pingali, Sai Venkatesh [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0000000179614176). 2025-08-11. Frameshifting Stimulatory Sequence Induces Large Structural Change of Ribosomal Proteins When Bound to E. coli Ribosomes. https://doi.org/10.1021/acs.biomac.4c01829

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DOE OSTI2026

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