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Co-translational binding of importins to nascent proteins

Various cellular quality control mechanisms support proteostasis. While, ribosome-associated chaperones prevent the misfolding of nascent chains during translation, importins were shown to prevent the aggregation of specific cargoes in a post-translational mechanism prior the import into the nucleop...

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Autores principales: Seidel, Maximilian, Romanov, Natalie, Obarska-Kosinska, Agnieszka, Becker, Anja, Trevisan Doimo de Azevedo, Nayara, Provaznik, Jan, Nagaraja, Sankarshana R., Landry, Jonathan J. M., Benes, Vladimir, Beck, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10256725/
https://www.ncbi.nlm.nih.gov/pubmed/37296145
http://dx.doi.org/10.1038/s41467-023-39150-9
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author Seidel, Maximilian
Romanov, Natalie
Obarska-Kosinska, Agnieszka
Becker, Anja
Trevisan Doimo de Azevedo, Nayara
Provaznik, Jan
Nagaraja, Sankarshana R.
Landry, Jonathan J. M.
Benes, Vladimir
Beck, Martin
author_facet Seidel, Maximilian
Romanov, Natalie
Obarska-Kosinska, Agnieszka
Becker, Anja
Trevisan Doimo de Azevedo, Nayara
Provaznik, Jan
Nagaraja, Sankarshana R.
Landry, Jonathan J. M.
Benes, Vladimir
Beck, Martin
author_sort Seidel, Maximilian
collection PubMed
description Various cellular quality control mechanisms support proteostasis. While, ribosome-associated chaperones prevent the misfolding of nascent chains during translation, importins were shown to prevent the aggregation of specific cargoes in a post-translational mechanism prior the import into the nucleoplasm. Here, we hypothesize that importins may already bind ribosome-associated cargo in a co-translational manner. We systematically measure the nascent chain association of all importins in Saccharomyces cerevisiae by selective ribosome profiling. We identify a subset of importins that bind to a wide range of nascent, often uncharacterized cargoes. This includes ribosomal proteins, chromatin remodelers and RNA binding proteins that are aggregation prone in the cytosol. We show that importins act consecutively with other ribosome-associated chaperones. Thus, the nuclear import system is directly intertwined with nascent chain folding and chaperoning.
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spelling pubmed-102567252023-06-11 Co-translational binding of importins to nascent proteins Seidel, Maximilian Romanov, Natalie Obarska-Kosinska, Agnieszka Becker, Anja Trevisan Doimo de Azevedo, Nayara Provaznik, Jan Nagaraja, Sankarshana R. Landry, Jonathan J. M. Benes, Vladimir Beck, Martin Nat Commun Article Various cellular quality control mechanisms support proteostasis. While, ribosome-associated chaperones prevent the misfolding of nascent chains during translation, importins were shown to prevent the aggregation of specific cargoes in a post-translational mechanism prior the import into the nucleoplasm. Here, we hypothesize that importins may already bind ribosome-associated cargo in a co-translational manner. We systematically measure the nascent chain association of all importins in Saccharomyces cerevisiae by selective ribosome profiling. We identify a subset of importins that bind to a wide range of nascent, often uncharacterized cargoes. This includes ribosomal proteins, chromatin remodelers and RNA binding proteins that are aggregation prone in the cytosol. We show that importins act consecutively with other ribosome-associated chaperones. Thus, the nuclear import system is directly intertwined with nascent chain folding and chaperoning. Nature Publishing Group UK 2023-06-09 /pmc/articles/PMC10256725/ /pubmed/37296145 http://dx.doi.org/10.1038/s41467-023-39150-9 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Seidel, Maximilian
Romanov, Natalie
Obarska-Kosinska, Agnieszka
Becker, Anja
Trevisan Doimo de Azevedo, Nayara
Provaznik, Jan
Nagaraja, Sankarshana R.
Landry, Jonathan J. M.
Benes, Vladimir
Beck, Martin
Co-translational binding of importins to nascent proteins
title Co-translational binding of importins to nascent proteins
title_full Co-translational binding of importins to nascent proteins
title_fullStr Co-translational binding of importins to nascent proteins
title_full_unstemmed Co-translational binding of importins to nascent proteins
title_short Co-translational binding of importins to nascent proteins
title_sort co-translational binding of importins to nascent proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10256725/
https://www.ncbi.nlm.nih.gov/pubmed/37296145
http://dx.doi.org/10.1038/s41467-023-39150-9
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