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Updated: Apr 19, 2026

Rapid Isolation of the Mitoribosome from HEK Cells
Published on: October 4, 2018
Another look at mutations in ribosomal protein S4 lends strong support to the domain closure model
1Department of Microbiology, Ohio State Biochemistry Program, and Center for RNA Biology, Ohio State University, Columbus, Ohio, USA fredrick.5@osu.edu.
Abstract:
Ribosomes employ a "kinetic discrimination" mechanism, in which correct substrates are incorporated more rapidly than incorrect ones. The structural basis of this mechanism may involve 30S domain closure, a global conformational change that coincides with codon recognition. In a direct screen for fidelity-altering mutations, Agarwal and coworkers (D. Agarwal, D. Kamath, S. T. Gregory, and M. O'Connor, J Bacteriol 197:1017-1025, 2015, doi:10.1128/JB.02485-14) isolated mutations that progressively truncate the C terminus of S4. All of these promote miscoding and undoubtedly destabilize the S4-S5 interface, consistent with the domain closure model.
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