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The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus
Stockholm University, Science for Life Laboratory (SciLifeLab). Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 8
2017 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 8, 723Article in journal (Refereed) Published
Abstract [en]

Formation of 100S ribosome dimer is generally associated with translation suppression in bacteria. Trans-acting factors ribosome modulation factor (RMF) and hibernating promoting factor (HPF) were shown to directly mediate this process in E. coli. Gram-positive S. aureus lacks an RMF homolog and the structural basis for its 100S formation was not known. Here we report the cryo-electron microscopy structure of the native 100S ribosome from S. aureus, revealing the molecular mechanism of its formation. The structure is distinct from previously reported analogs and relies on the HPF C-terminal extension forming the binding platform for the interactions between both of the small ribosomal subunits. The 100S dimer is formed through interactions between rRNA h26, h40, and protein uS2, involving conformational changes of the head as well as surface regions that could potentially prevent RNA polymerase from docking to the ribosome.

Place, publisher, year, edition, pages
2017. Vol. 8, 723
Keyword [en]
Bacterial structural biology, Cryoelectron microscopy, Ribosomal proteins, Ribosome
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-148070DOI: 10.1038/s41467-017-00753-8ISI: 000411989800007PubMedID: 28959035OAI: oai:DiVA.org:su-148070DiVA: diva2:1152614
Available from: 2017-10-25 Created: 2017-10-25 Last updated: 2017-11-29Bibliographically approved

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Aibara, ShintaroAmunts, Alexey
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Science for Life Laboratory (SciLifeLab)Department of Biochemistry and Biophysics
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