The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus

Donna Matzov, Shintaro Aibara, Arnab Basu, Ella Zimmerman, Anat Bashan, Mee-Ngan F. Yap (), Alexey Amunts () and Ada E. Yonath ()
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Donna Matzov: The Weizmann Institute of Science
Shintaro Aibara: Stockholm University
Arnab Basu: Saint Louis University School of Medicine
Ella Zimmerman: The Weizmann Institute of Science
Anat Bashan: The Weizmann Institute of Science
Mee-Ngan F. Yap: Saint Louis University School of Medicine
Alexey Amunts: Stockholm University
Ada E. Yonath: The Weizmann Institute of Science

Nature Communications, 2017, vol. 8, issue 1, 1-7

Abstract: Abstract 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.

Date: 2017
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DOI: 10.1038/s41467-017-00753-8

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