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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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

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spelling	doaj-5462b5389ea14028988762da9a1a55f42021-05-11T07:22:06ZengNature Publishing GroupNature Communications2041-17232017-09-01811710.1038/s41467-017-00753-8The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureusDonna Matzov0Shintaro Aibara1Arnab Basu2Ella Zimmerman3Anat Bashan4Mee-Ngan F. Yap5Alexey Amunts6Ada E. Yonath7Faculty of Chemistry, Department of Structural Biology, The Weizmann Institute of ScienceScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm UniversityEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of MedicineFaculty of Chemistry, Department of Structural Biology, The Weizmann Institute of ScienceFaculty of Chemistry, Department of Structural Biology, The Weizmann Institute of ScienceEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of MedicineScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm UniversityFaculty of Chemistry, Department of Structural Biology, The Weizmann Institute of ScienceUnder 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.https://doi.org/10.1038/s41467-017-00753-8
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Donna Matzov Shintaro Aibara Arnab Basu Ella Zimmerman Anat Bashan Mee-Ngan F. Yap Alexey Amunts Ada E. Yonath
spellingShingle	Donna Matzov Shintaro Aibara Arnab Basu Ella Zimmerman Anat Bashan Mee-Ngan F. Yap Alexey Amunts Ada E. Yonath The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus Nature Communications
author_facet	Donna Matzov Shintaro Aibara Arnab Basu Ella Zimmerman Anat Bashan Mee-Ngan F. Yap Alexey Amunts Ada E. Yonath
author_sort	Donna Matzov
title	The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus
title_short	The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus
title_full	The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus
title_fullStr	The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus
title_full_unstemmed	The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus
title_sort	cryo-em structure of hibernating 100s ribosome dimer from pathogenic staphylococcus aureus
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2017-09-01
description	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.
url	https://doi.org/10.1038/s41467-017-00753-8
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The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus

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