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...
Main Authors: | , , , , , , , |
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Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2017-09-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-017-00753-8 |
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. |
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ISSN: | 2041-1723 |