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  Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1

Beckert, B., Turk, M., Czech, A., Berninghausen, O., Beckmann, R., Ignatova, Z., et al. (2018). Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1. Nature Microbiology, 3(10), 1115-1121. doi:10.1038/s41564-018-0237-0.

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 Creators:
Beckert, Bertrand1, Author
Turk, Martin2, Author              
Czech, Andreas1, Author
Berninghausen, Otto1, Author
Beckmann, Roland1, Author
Ignatova, Zoya1, Author
Plitzko, Jürgen M.2, Author              
Wilson, Daniel N.1, Author
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: PHASE ESCHERICHIA-COLI; STATIONARY-PHASE; ELECTRON CRYOMICROSCOPY; MESSENGER-RNA; CRYO-EM; TRANSLATION INITIATION; IN-VITRO; BINDING; STRESS; YFIAMicrobiology;
 Abstract: To survive under conditions of stress, such as nutrient deprivation, bacterial 70S ribosomes dimerize to form hibernating 100S particles(1). In gamma-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 angstrom and 7.9 angstrom 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 Grampositive bacteria(5-8), and reveals a unique role for bS1 in translation regulation.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000448228400009
DOI: 10.1038/s41564-018-0237-0
 Degree: -

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Title: Nature Microbiology
  Abbreviation : Nat. Microbiol.
Source Genre: Journal
 Creator(s):
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Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 3 (10) Sequence Number: - Start / End Page: 1115 - 1121 Identifier: Other: 2058-5276
CoNE: https://pure.mpg.de/cone/journals/resource/2058-5276