Visualizing the transfer-messenger RNA as the ribosome resumes translation

Jie Fu, Yaser Hashem, Iwona Wower, Jianlin Lei, Hstau Y. Liao, Christian Zwieb, Jacek Wower, Joachim Frank

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


Bacterial ribosomes stalled by truncated mRNAs are rescued by transfer-messenger RNA (tmRNA), a dual-function molecule that contains a tRNA-like domain (TLD) and an internal open reading frame (ORF). Occupying the empty A site with its TLD, the tmRNA enters the ribosome with the help of elongation factor Tu and a protein factor called small protein B (SmpB), and switches the translation to its own ORF. In this study, using cryo-electron microscopy, we obtained the first structure of an in vivo-formed complex containing ribosome and the tmRNA at the point where the TLD is accommodated into the ribosomal P site. We show that tmRNA maintains a stable arc and fork structure on the ribosome when its TLD moves to the ribosomal P site and translation resumes on its ORF. Based on the density map, we built an atomic model, which suggests that SmpB interacts with the five nucleotides immediately upstream of the resume codon, thereby determining the correct selection of the reading frame on the ORF of tmRNA.

Original languageEnglish (US)
Pages (from-to)3819-3825
Number of pages7
JournalEMBO Journal
Issue number22
StatePublished - Nov 17 2010
Externally publishedYes


  • SmpB
  • tmRNA
  • trans-translation

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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