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Updated: Aug 24, 2026

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
Published on: February 25, 2011
tRNA slippage at the tmRNA resume codon
Michael J Trimble1, Amy Minnicus, Kelly P Williams
1Department of Biology, Indiana University, Bloomington, IN 47405, USA.
Unlabelled:
The bacterial ribosome does not initiate translation on the mRNA portion of tmRNA; instead translation that had begun on a separate mRNA molecule resumes at a particular triplet on tmRNA (the resume codon). For at least two tRNAs that could pair with both the resume and -2 triplets on mutant tmRNAs, UAA (stop) as the second codon induced high-frequency -2 slippage on the resume codon in the P site. The frameshift product was not detected when the -2 base was altered. Deficiency for ribosomal L9 protein, which affects other cases of frameshifting, had no significant effect. A special feature of this frameshifting is its dependence on a particular context, that of the tmRNA resume codon; it failed on the same sequence in a regular mRNA, and, more strikingly, at the second tmRNA codon. This focuses attention on the peculiar features expected of the slippage-prone state, such as unusual E-site filling, that might make the P-site resume codon:anticodon interaction especially unstable.
Keywords:
tmRNA; ribosome; frameshift; E site; translation
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