Nature Microbiology, volume 3, issue 10, pages 1115-1121
Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1
Beckert Bertrand
1
,
Turk Martin
2
,
Czech Andreas
1
,
Berninghausen Otto
3
,
Beckmann Roland
3
,
Ignatova Zoya
1
,
Plitzko Juergen
2
,
1
Institute for Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany
|
2
Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
|
3
Gene Center, Department of Biochemistry and Center for integrated Protein Science Munich (CiPSM), Ludwig-Maximilians-Universität München, Munich, Germany
|
Publication type: Journal Article
Publication date: 2018-09-03
Cell Biology
Genetics
Microbiology (medical)
Microbiology
Applied Microbiology and Biotechnology
Immunology
Abstract
To survive under conditions of stress, such as nutrient deprivation, bacterial 70S ribosomes dimerize to form hibernating 100S particles1. In γ-proteobacteria, such as Escherichia coli, 100S formation requires the ribosome modulation factor (RMF) and the hibernation promoting factor (HPF)2–4. Here we present single-particle cryo-electron microscopy structures of hibernating 70S and 100S particles isolated from stationary-phase E. coli cells at 3.0 Å and 7.9 Å resolution, respectively. The structures reveal the binding sites for HPF and RMF as well as the unexpected presence of deacylated E-site transfer RNA and ribosomal protein bS1. HPF interacts with the anticodon-stem-loop of the E-tRNA and occludes the binding site for the messenger RNA as well as A- and P-site tRNAs. RMF facilitates stabilization of a compact conformation of bS1, which together sequester the anti-Shine-Dalgarno sequence of the 16S ribosomal RNA (rRNA), thereby inhibiting translation initiation. At the dimerization interface, the C-terminus of uS2 probes the mRNA entrance channel of the symmetry-related particle, thus suggesting that dimerization inactivates ribosomes by blocking the binding of mRNA within the channel. The back-to-back E. coli 100S arrangement is distinct from 100S particles observed previously in Gram-positive bacteria5–8, and reveals a unique role for bS1 in translation regulation.Cryo-electron-microscopy imaging of hibernating ribosomes from Escherichia coli elucidates the molecular composition of these complexes and their mode of assembly, reveals how translation initiation is inhibited, and identifies a role for the ribosomal protein S1 in ribosome inactivation.
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Beckert B. et al. Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1 // Nature Microbiology. 2018. Vol. 3. No. 10. pp. 1115-1121.
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Beckert B., Turk M., Czech A., Berninghausen O., Beckmann R., Ignatova Z., Plitzko J., Wilson D. W. Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1 // Nature Microbiology. 2018. Vol. 3. No. 10. pp. 1115-1121.
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TY - JOUR
DO - 10.1038/s41564-018-0237-0
UR - https://doi.org/10.1038%2Fs41564-018-0237-0
TI - Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1
T2 - Nature Microbiology
AU - Beckert, Bertrand
AU - Turk, Martin
AU - Czech, Andreas
AU - Berninghausen, Otto
AU - Beckmann, Roland
AU - Ignatova, Zoya
AU - Plitzko, Juergen
AU - Wilson, Daniel W.
PY - 2018
DA - 2018/09/03 00:00:00
PB - Springer Nature
SP - 1115-1121
IS - 10
VL - 3
SN - 2058-5276
ER -
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@article{2018_Beckert,
author = {Bertrand Beckert and Martin Turk and Andreas Czech and Otto Berninghausen and Roland Beckmann and Zoya Ignatova and Juergen Plitzko and Daniel W. Wilson},
title = {Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1},
journal = {Nature Microbiology},
year = {2018},
volume = {3},
publisher = {Springer Nature},
month = {sep},
url = {https://doi.org/10.1038%2Fs41564-018-0237-0},
number = {10},
pages = {1115--1121},
doi = {10.1038/s41564-018-0237-0}
}
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MLA
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Beckert, Bertrand, et al. “Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1.” Nature Microbiology, vol. 3, no. 10, Sep. 2018, pp. 1115-1121. https://doi.org/10.1038%2Fs41564-018-0237-0.