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

Under conditions of nutrient limitation, bacterial ribosomes undergo dimerization, forming a 100S complex that is translationally inactive. Here the authors present the structural basis for formation of the 100S complexes in Gram-positive bacteria, shedding light on the mechanism of translation supp...

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Bibliographic Details
Main Authors: Donna Matzov, Shintaro Aibara, Arnab Basu, Ella Zimmerman, Anat Bashan, Mee-Ngan F. Yap, Alexey Amunts, Ada E. Yonath
Format: Article
Language:English
Published: Nature Publishing Group 2017-09-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-00753-8
Description
Summary:Under conditions of nutrient limitation, bacterial ribosomes undergo dimerization, forming a 100S complex that is translationally inactive. Here the authors present the structural basis for formation of the 100S complexes in Gram-positive bacteria, shedding light on the mechanism of translation suppression by the ribosome-silencing factors.
ISSN:2041-1723