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, Lital Alfonta

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

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.

Original languageEnglish
Article number4827
JournalNature Communications
Volume11
Issue number1
DOIs
StatePublished - 1 Dec 2020

Fingerprint

Dive into the research topics of 'A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon'. Together they form a unique fingerprint.

Cite this