A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon
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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. The mechanisms for regulating translation re-initiation in bacteria remain poorly understood. Here, the authors screened a library of synthetic operons and identified a ribosome termination structure that modulates re-initiation efficiency and which is conserved across bacteria.
Originalsprog | Engelsk |
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Artikelnummer | 4827 |
Tidsskrift | Nature Communications |
Vol/bind | 11 |
Udgave nummer | 1 |
Antal sider | 11 |
ISSN | 2041-1723 |
DOI | |
Status | Udgivet - 24 sep. 2020 |
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