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A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon

Author

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  • Yonatan Chemla

    (Ben-Gurion University of the Negev
    Ben-Gurion University of the Negev
    Ben-Gurion University of the Negev)

  • Michael Peeri

    (Tel Aviv University)

  • Mathias Luidor Heltberg

    (University of Copenhagen)

  • Jerry Eichler

    (Ben-Gurion University of the Negev)

  • Mogens Høgh Jensen

    (University of Copenhagen)

  • Tamir Tuller

    (Tel Aviv University)

  • Lital Alfonta

    (Ben-Gurion University of the Negev
    Ben-Gurion University of the Negev
    Ben-Gurion University of the Negev)

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.

Suggested Citation

  • Yonatan Chemla & Michael Peeri & Mathias Luidor Heltberg & Jerry Eichler & Mogens Høgh Jensen & Tamir Tuller & Lital Alfonta, 2020. "A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18577-4
    DOI: 10.1038/s41467-020-18577-4
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