title: Another look at mutations in ribosomal protein S4 lends strong support to the domain closure model.
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.
authors.affiliation: Department of Microbiology, Ohio State Biochemistry Program, and Center for RNA Biology, Ohio State University, Columbus, Ohio, USA fredrick.5@osu.edu.
authors.forename: Kurt
authors.initials: K
authors.lastname: Fredrick
mesh_terms: D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*
chemical_list: D029968:Escherichia coli Proteins; D012269:Ribosomal Proteins; C031798:ribosomal protein S4; C030831:ribosomal protein S5