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Updated: Dec 7, 2025

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
Published on: February 12, 2022
A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon
Yonatan Chemla1,2,3, Michael Peeri4, Mathias Luidor Heltberg5
1Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva, 8410501, Israel.
Abstract:
In bacteria, translation re-initiation is crucial for synthesizing proteins encoded by genes that are organized into operons. The mechanisms regulating translation re-initiation remain, however, poorly understood. We now describe the ribosome termination structure (RTS), a conserved and stable mRNA secondary structure localized immediately downstream of stop codons, and provide experimental evidence for its role in governing re-initiation efficiency in a synthetic Escherichia coli operon. We further report that RTSs are abundant, being associated with 18%-65% of genes in 128 analyzed bacterial genomes representing all phyla, and are selectively depleted when translation re-initiation is advantageous yet selectively enriched so as to insulate translation when re-initiation is deleterious. Our results support a potentially universal role for the RTS in controlling translation termination-insulation and re-initiation across bacteria.
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