A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon
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A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon. / Chemla, Yonatan; Peeri, Michael; Heltberg, Mathias Luidor; Eichler, Jerry; Jensen, Mogens Hogh; Tuller, Tamir; Alfonta, Lital.
In: Nature Communications, Vol. 11, No. 1, 4827, 24.09.2020.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon
AU - Chemla, Yonatan
AU - Peeri, Michael
AU - Heltberg, Mathias Luidor
AU - Eichler, Jerry
AU - Jensen, Mogens Hogh
AU - Tuller, Tamir
AU - Alfonta, Lital
PY - 2020/9/24
Y1 - 2020/9/24
N2 - 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.
AB - 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.
KW - INITIATION
KW - REINITIATION
KW - ABUNDANCE
KW - DATABASE
U2 - 10.1038/s41467-020-18577-4
DO - 10.1038/s41467-020-18577-4
M3 - Journal article
C2 - 32973167
VL - 11
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1
M1 - 4827
ER -
ID: 249903552