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Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy
As one of the most prevalent post‐translational modifications in eukaryotic cells, ubiquitylation plays vital roles in many cellular processes, such as protein degradation, DNA metabolism, and cell differentiation. Substrate proteins can be tagged by distinct types of polymeric ubiquitin (Ub) chains...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6771822/ https://www.ncbi.nlm.nih.gov/pubmed/30920720 http://dx.doi.org/10.1002/cbic.201900146 |
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author | Zhao, Xiaohui Mißun, Maite Schneider, Tobias Müller, Franziska Lutz, Joachim Scheffner, Martin Marx, Andreas Kovermann, Michael |
author_facet | Zhao, Xiaohui Mißun, Maite Schneider, Tobias Müller, Franziska Lutz, Joachim Scheffner, Martin Marx, Andreas Kovermann, Michael |
author_sort | Zhao, Xiaohui |
collection | PubMed |
description | As one of the most prevalent post‐translational modifications in eukaryotic cells, ubiquitylation plays vital roles in many cellular processes, such as protein degradation, DNA metabolism, and cell differentiation. Substrate proteins can be tagged by distinct types of polymeric ubiquitin (Ub) chains, which determine the eventual fate of the modified protein. A facile, click chemistry based approach for the efficient generation of linkage‐defined Ub chains, including Ub dimers, was recently established. Within these chains, individual Ub moieties are connected through a triazole linkage, rather than the natural isopeptide bond. Herein, it is reported that the conformation of an artificially K48‐linked Ub dimer resembles that of the natively linked dimer, with respect to structural and dynamic characteristics, as demonstrated by means of high‐resolution NMR spectroscopy. Thus, it is proposed that artificially linked Ub dimers, as generated by this approach, represent potent tools for studying the inherently different properties and functions of distinct Ub chains. |
format | Online Article Text |
id | pubmed-6771822 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-67718222019-10-07 Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy Zhao, Xiaohui Mißun, Maite Schneider, Tobias Müller, Franziska Lutz, Joachim Scheffner, Martin Marx, Andreas Kovermann, Michael Chembiochem Communications As one of the most prevalent post‐translational modifications in eukaryotic cells, ubiquitylation plays vital roles in many cellular processes, such as protein degradation, DNA metabolism, and cell differentiation. Substrate proteins can be tagged by distinct types of polymeric ubiquitin (Ub) chains, which determine the eventual fate of the modified protein. A facile, click chemistry based approach for the efficient generation of linkage‐defined Ub chains, including Ub dimers, was recently established. Within these chains, individual Ub moieties are connected through a triazole linkage, rather than the natural isopeptide bond. Herein, it is reported that the conformation of an artificially K48‐linked Ub dimer resembles that of the natively linked dimer, with respect to structural and dynamic characteristics, as demonstrated by means of high‐resolution NMR spectroscopy. Thus, it is proposed that artificially linked Ub dimers, as generated by this approach, represent potent tools for studying the inherently different properties and functions of distinct Ub chains. John Wiley and Sons Inc. 2019-06-24 2019-07-15 /pmc/articles/PMC6771822/ /pubmed/30920720 http://dx.doi.org/10.1002/cbic.201900146 Text en © 2019 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Communications Zhao, Xiaohui Mißun, Maite Schneider, Tobias Müller, Franziska Lutz, Joachim Scheffner, Martin Marx, Andreas Kovermann, Michael Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy |
title | Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy |
title_full | Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy |
title_fullStr | Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy |
title_full_unstemmed | Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy |
title_short | Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy |
title_sort | artificially linked ubiquitin dimers characterised structurally and dynamically by nmr spectroscopy |
topic | Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6771822/ https://www.ncbi.nlm.nih.gov/pubmed/30920720 http://dx.doi.org/10.1002/cbic.201900146 |
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