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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2020-09-24

AUTHORS

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

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. More... »

PAGES

4827

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-020-18577-4

DOI

http://dx.doi.org/10.1038/s41467-020-18577-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1131133661

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/32973167


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