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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Autores principales:	Donna Matzov, Shintaro Aibara, Arnab Basu, Ella Zimmerman, Anat Bashan, Mee-Ngan F. Yap, Alexey Amunts, Ada E. Yonath
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5462b5389ea14028988762da9a1a55f4
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spelling	oai:doaj.org-article:5462b5389ea14028988762da9a1a55f42021-12-02T15:38:55ZThe cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus10.1038/s41467-017-00753-82041-1723https://doaj.org/article/5462b5389ea14028988762da9a1a55f42017-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00753-8https://doaj.org/toc/2041-1723Under 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.Donna MatzovShintaro AibaraArnab BasuElla ZimmermanAnat BashanMee-Ngan F. YapAlexey AmuntsAda E. YonathNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-7 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
author	Donna Matzov Shintaro Aibara Arnab Basu Ella Zimmerman Anat Bashan Mee-Ngan F. Yap Alexey Amunts Ada E. Yonath
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 Portfolio
publishDate	2017
url	https://doaj.org/article/5462b5389ea14028988762da9a1a55f4
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The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus

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