The central role of protein S12 in organizing the structure of the decoding site of the ribosome

H. Demirci,Leyi Wang,F. Murphy,E. Murphy,Jennifer F Carr,S. Blanchard,G. Jogl,A. E. Dahlberg,S. T. Gregory

Published 2013 in RNA: A publication of the RNA Society

ABSTRACT

Structural studies on the ribosome have provided tremendous insights into how cognate codon–anticodon interactions in the decoding center lead to tRNA selection and, ultimately, to peptide chain elongation. Here, in the genetically and structurally tractable organism Thermus thermophilus, the authors isolate and identify streptomycin-dependent (SmD) ribosomal variants, as well as streptomycin-independent (SmI) revertants, with mutations affecting ribosomal protein S12 and the 16S rRNA, respectively. Single-molecule FRET and structural studies reveal here how these decoding-site proximal mutations can impact the ability of ribosomes to reach the GTPase-activated state required for progression in tRNA selection.

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