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

doi:10.1038/s41467-020-18577-4

Nature Communications (Sep 2020)

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

Affiliations

Yonatan Chemla: Department of Chemistry, Ben-Gurion University of the Negev
Michael Peeri: Department of Biomedical Engineering, The Iby and Aladar Fleischman Faculty of Engineering and The Sagol School of Neuroscience, Tel Aviv University
Mathias Luidor Heltberg: Niels Bohr Institute, University of Copenhagen
Jerry Eichler: Department of Life Sciences, Ben-Gurion University of the Negev
Mogens Høgh Jensen: Niels Bohr Institute, University of Copenhagen
Tamir Tuller: Department of Biomedical Engineering, The Iby and Aladar Fleischman Faculty of Engineering and The Sagol School of Neuroscience, Tel Aviv University
Lital Alfonta: Department of Chemistry, Ben-Gurion University of the Negev

DOI: https://doi.org/10.1038/s41467-020-18577-4
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 11

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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