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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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

Harvard

Chemla, Y, Peeri, M, Heltberg, ML, Eichler, J, Jensen, MH, Tuller, T & Alfonta, L 2020, 'A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon', Nature Communications, vol. 11, no. 1, 4827. https://doi.org/10.1038/s41467-020-18577-4

APA

Chemla, Y., Peeri, M., Heltberg, M. L., Eichler, J., Jensen, M. H., Tuller, T., & Alfonta, L. (2020). A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon. Nature Communications, 11(1), [4827]. https://doi.org/10.1038/s41467-020-18577-4

Vancouver

Chemla Y, Peeri M, Heltberg ML, Eichler J, Jensen MH, Tuller T et al. A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon. Nature Communications. 2020 Sep 24;11(1). 4827. https://doi.org/10.1038/s41467-020-18577-4

Author

Chemla, Yonatan ; Peeri, Michael ; Heltberg, Mathias Luidor ; Eichler, Jerry ; Jensen, Mogens Hogh ; Tuller, Tamir ; Alfonta, Lital. / A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon. In: Nature Communications. 2020 ; Vol. 11, No. 1.

Bibtex

@article{66e93b26084842afa29f1ff624934e24,
title = "A possible universal role for mRNA secondary structure in bacterial translation revealed using a synthetic operon",
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. 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.",
keywords = "INITIATION, REINITIATION, ABUNDANCE, DATABASE",
author = "Yonatan Chemla and Michael Peeri and Heltberg, {Mathias Luidor} and Jerry Eichler and Jensen, {Mogens Hogh} and Tamir Tuller and Lital Alfonta",
year = "2020",
month = sep,
day = "24",
doi = "10.1038/s41467-020-18577-4",
language = "English",
volume = "11",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

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