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

Yonatan ChemlaMichael PeeriMathias Luidor HeltbergJerry EichlerMogens Høgh JensenTamir TullerLital Alfonta
Published in: Nature communications (2020)
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.
Keyphrases
  • escherichia coli
  • genome wide
  • single cell
  • staphylococcus aureus
  • multidrug resistant
  • binding protein
  • biofilm formation