Deciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy

Abstract The eukaryotic ribosome-associated complex (RAC) plays a significant role in de novo protein folding. Its unique interaction with the ribosome, comprising contacts to both ribosomal subunits, suggests a RAC-mediated coordination between translation elongation and co-translational protein fo...

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Autores principales:	Sandra J. Fries, Theresa S. Braun, Christoph Globisch, Christine Peter, Malte Drescher, Elke Deuerling
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/abd6bff357c04ad59b98e16224bbcb52
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spelling	oai:doaj.org-article:abd6bff357c04ad59b98e16224bbcb522021-12-02T18:27:46ZDeciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy10.1038/s41598-021-87847-y2045-2322https://doaj.org/article/abd6bff357c04ad59b98e16224bbcb522021-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-87847-yhttps://doaj.org/toc/2045-2322Abstract The eukaryotic ribosome-associated complex (RAC) plays a significant role in de novo protein folding. Its unique interaction with the ribosome, comprising contacts to both ribosomal subunits, suggests a RAC-mediated coordination between translation elongation and co-translational protein folding. Here, we apply electron paramagnetic resonance (EPR) spectroscopy combined with site-directed spin labeling (SDSL) to gain deeper insights into a RAC–ribosome contact affecting translational accuracy. We identified a local contact point of RAC to the ribosome. The data provide the first experimental evidence for the existence of a four-helix bundle as well as a long α-helix in full-length RAC, in solution as well as on the ribosome. Additionally, we complemented the structural picture of the region mediating this functionally important contact on the 40S ribosomal subunit. In sum, this study constitutes the first application of SDSL-EPR spectroscopy to elucidate the molecular details of the interaction between the 3.3 MDa translation machinery and a chaperone complex.Sandra J. FriesTheresa S. BraunChristoph GlobischChristine PeterMalte DrescherElke DeuerlingNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sandra J. Fries Theresa S. Braun Christoph Globisch Christine Peter Malte Drescher Elke Deuerling Deciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy
description	Abstract The eukaryotic ribosome-associated complex (RAC) plays a significant role in de novo protein folding. Its unique interaction with the ribosome, comprising contacts to both ribosomal subunits, suggests a RAC-mediated coordination between translation elongation and co-translational protein folding. Here, we apply electron paramagnetic resonance (EPR) spectroscopy combined with site-directed spin labeling (SDSL) to gain deeper insights into a RAC–ribosome contact affecting translational accuracy. We identified a local contact point of RAC to the ribosome. The data provide the first experimental evidence for the existence of a four-helix bundle as well as a long α-helix in full-length RAC, in solution as well as on the ribosome. Additionally, we complemented the structural picture of the region mediating this functionally important contact on the 40S ribosomal subunit. In sum, this study constitutes the first application of SDSL-EPR spectroscopy to elucidate the molecular details of the interaction between the 3.3 MDa translation machinery and a chaperone complex.
format	article
author	Sandra J. Fries Theresa S. Braun Christoph Globisch Christine Peter Malte Drescher Elke Deuerling
author_facet	Sandra J. Fries Theresa S. Braun Christoph Globisch Christine Peter Malte Drescher Elke Deuerling
author_sort	Sandra J. Fries
title	Deciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy
title_short	Deciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy
title_full	Deciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy
title_fullStr	Deciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy
title_full_unstemmed	Deciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy
title_sort	deciphering molecular details of the rac–ribosome interaction by epr spectroscopy
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/abd6bff357c04ad59b98e16224bbcb52
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Deciphering molecular details of the RAC–ribosome interaction by EPR spectroscopy

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