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

Yonatan Chemla, Michael Peeri, Mathias Luidor Heltberg, Jerry Eichler, Mogens Høgh Jensen, Tamir Tuller () and Lital Alfonta ()
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Yonatan Chemla: 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

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: 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.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18577-4

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DOI: 10.1038/s41467-020-18577-4

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