Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation

Translation within mitochondria is carried out by specialized mitoribosomes and translational factors. Here the authors describe cryo-EM structures of the human mitochondrial translation elongation factor G1 in complex with human mitoribosomes, revealing distinct mechanism that include conformationa...

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Autores principales:	Ravi Kiran Koripella, Manjuli R. Sharma, Kalpana Bhargava, Partha P. Datta, Prem S. Kaushal, Pooja Keshavan, Linda L. Spremulli, Nilesh K. Banavali, Rajendra K. Agrawal
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7811cccf65184e81a96fed86561d888f
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spelling	oai:doaj.org-article:7811cccf65184e81a96fed86561d888f2021-12-02T16:31:53ZStructures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation10.1038/s41467-020-17715-22041-1723https://doaj.org/article/7811cccf65184e81a96fed86561d888f2020-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17715-2https://doaj.org/toc/2041-1723Translation within mitochondria is carried out by specialized mitoribosomes and translational factors. Here the authors describe cryo-EM structures of the human mitochondrial translation elongation factor G1 in complex with human mitoribosomes, revealing distinct mechanism that include conformational changes at the polypeptide exit tunnel.Ravi Kiran KoripellaManjuli R. SharmaKalpana BhargavaPartha P. DattaPrem S. KaushalPooja KeshavanLinda L. SpremulliNilesh K. BanavaliRajendra K. AgrawalNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ravi Kiran Koripella Manjuli R. Sharma Kalpana Bhargava Partha P. Datta Prem S. Kaushal Pooja Keshavan Linda L. Spremulli Nilesh K. Banavali Rajendra K. Agrawal Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation
description	Translation within mitochondria is carried out by specialized mitoribosomes and translational factors. Here the authors describe cryo-EM structures of the human mitochondrial translation elongation factor G1 in complex with human mitoribosomes, revealing distinct mechanism that include conformational changes at the polypeptide exit tunnel.
format	article
author	Ravi Kiran Koripella Manjuli R. Sharma Kalpana Bhargava Partha P. Datta Prem S. Kaushal Pooja Keshavan Linda L. Spremulli Nilesh K. Banavali Rajendra K. Agrawal
author_facet	Ravi Kiran Koripella Manjuli R. Sharma Kalpana Bhargava Partha P. Datta Prem S. Kaushal Pooja Keshavan Linda L. Spremulli Nilesh K. Banavali Rajendra K. Agrawal
author_sort	Ravi Kiran Koripella
title	Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation
title_short	Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation
title_full	Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation
title_fullStr	Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation
title_full_unstemmed	Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation
title_sort	structures of the human mitochondrial ribosome bound to ef-g1 reveal distinct features of mitochondrial translation elongation
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/7811cccf65184e81a96fed86561d888f
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Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation

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