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Updated: Jul 17, 2026

Real-time Imaging of Single Engineered RNA Transcripts in Living Cells Using Ratiometric Bimolecular Beacons
Published on: August 6, 2014
Visualizing tmRNA entry into a stalled ribosome
Mikel Valle1, Reynald Gillet, Sukhjit Kaur
1Howard Hughes Medical Institute, Wadsworth Center, Health Research, Inc., Empire State Plaza, Albany, NY 12201-0509, USA.
Abstract:
Bacterial ribosomes stalled on defective messenger RNAs (mRNAs) are rescued by tmRNA, an approximately 300-nucleotide-long molecule that functions as both transfer RNA (tRNA) and mRNA. Translation then switches from the defective message to a short open reading frame on tmRNA that tags the defective nascent peptide chain for degradation. However, the mechanism by which tmRNA can enter and move through the ribosome is unknown. We present a cryo-electron microscopy study at approximately 13 to 15 angstroms of the entry of tmRNA into the ribosome. The structure reveals how tmRNA could move through the ribosome despite its complicated topology and also suggests roles for proteins S1 and SmpB in the function of tmRNA.
Insights
Bacterial ribosomes use tmRNA (transfer and messenger RNA) to rescue stalled translation. This study reveals tmRNA
Area of Science:
- Molecular Biology
- Structural Biology
- Microbiology
Background:
- Bacterial ribosomes stall on defective messenger RNAs (mRNAs).
- tmRNA rescues stalled ribosomes by acting as both transfer RNA (tRNA) and mRNA.
- tmRNA facilitates tagging of nascent peptides for degradation.
Purpose of the Study:
- To elucidate the mechanism of tmRNA entry and movement within the bacterial ribosome.
- To understand how tmRNA navigates its complex topology inside the ribosome.
Main Methods:
- Cryo-electron microscopy (cryo-EM) was used to determine the structure of tmRNA interacting with the ribosome.
- High-resolution structural analysis at approximately 13-15 angstroms.
Main Results:
- The cryo-EM structure reveals the detailed pathway of tmRNA entry into the ribosome.
- The structure explains how tmRNA's complex topology allows it to traverse the ribosome.
- The study suggests specific roles for proteins S1 and SmpB in tmRNA-mediated ribosome rescue.
Conclusions:
- The structural insights provide a mechanistic understanding of tmRNA's ribosome entry and translocation.
- Proteins S1 and SmpB are implicated as key players in tmRNA function.
- This work clarifies a fundamental process in bacterial translational quality control.
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