Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism

Rasmus Kock Flygaard; Niels Boegholm; Marat Yusupov; Lasse B. Jenner

doi:10.1038/s41467-018-06724-x

Nature Communications (Oct 2018)

Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism

Rasmus Kock Flygaard,
Niels Boegholm,
Marat Yusupov,
Lasse B. Jenner

Affiliations

Rasmus Kock Flygaard: Department of Molecular Biology and Genetics, Aarhus University
Niels Boegholm: Department of Molecular Biology and Genetics, Aarhus University
Marat Yusupov: Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, CNRS UMR710, INSERM U964, University of Strasbourg
Lasse B. Jenner: Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, CNRS UMR710, INSERM U964, University of Strasbourg

DOI: https://doi.org/10.1038/s41467-018-06724-x
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 12

Abstract

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During stress conditions bacterial ribosomes dimerize and form inactive but stable hibernating 100S particles, a process that is facilitated by the hibernation-promoting factor (HPF). Here the authors analyze 100S dimer formation as a function of HPF protein concentration and present the Thermus thermophilus 100S ribosome cryo-EM structure.

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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