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Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius
In eukaryotes, the covalent attachment of ubiquitin chains directs substrates to the proteasome for degradation. Recently, ubiquitin-like modifications have also been described in the archaeal domain of life. It has subsequently been hypothesized that ubiquitin-like proteasomal degradation might als...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4569737/ https://www.ncbi.nlm.nih.gov/pubmed/26348592 http://dx.doi.org/10.1038/ncomms9163 |
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author | Anjum, Rana S. Bray, Sian M. Blackwood, John K. Kilkenny, Mairi L. Coelho, Matthew A. Foster, Benjamin M. Li, Shurong Howard, Julie A. Pellegrini, Luca Albers, Sonja-Verena Deery, Michael J. Robinson, Nicholas P. |
author_facet | Anjum, Rana S. Bray, Sian M. Blackwood, John K. Kilkenny, Mairi L. Coelho, Matthew A. Foster, Benjamin M. Li, Shurong Howard, Julie A. Pellegrini, Luca Albers, Sonja-Verena Deery, Michael J. Robinson, Nicholas P. |
author_sort | Anjum, Rana S. |
collection | PubMed |
description | In eukaryotes, the covalent attachment of ubiquitin chains directs substrates to the proteasome for degradation. Recently, ubiquitin-like modifications have also been described in the archaeal domain of life. It has subsequently been hypothesized that ubiquitin-like proteasomal degradation might also operate in these microbes, since all archaeal species utilize homologues of the eukaryotic proteasome. Here we perform a structural and biochemical analysis of a ubiquitin-like modification pathway in the archaeon Sulfolobus acidocaldarius. We reveal that this modifier is homologous to the eukaryotic ubiquitin-related modifier Urm1, considered to be a close evolutionary relative of the progenitor of all ubiquitin-like proteins. Furthermore we demonstrate that urmylated substrates are recognized and processed by the archaeal proteasome, by virtue of a direct interaction with the modifier. Thus, the regulation of protein stability by Urm1 and the proteasome in archaea is likely representative of an ancient pathway from which eukaryotic ubiquitin-mediated proteolysis has evolved. |
format | Online Article Text |
id | pubmed-4569737 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Pub. Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-45697372015-09-28 Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius Anjum, Rana S. Bray, Sian M. Blackwood, John K. Kilkenny, Mairi L. Coelho, Matthew A. Foster, Benjamin M. Li, Shurong Howard, Julie A. Pellegrini, Luca Albers, Sonja-Verena Deery, Michael J. Robinson, Nicholas P. Nat Commun Article In eukaryotes, the covalent attachment of ubiquitin chains directs substrates to the proteasome for degradation. Recently, ubiquitin-like modifications have also been described in the archaeal domain of life. It has subsequently been hypothesized that ubiquitin-like proteasomal degradation might also operate in these microbes, since all archaeal species utilize homologues of the eukaryotic proteasome. Here we perform a structural and biochemical analysis of a ubiquitin-like modification pathway in the archaeon Sulfolobus acidocaldarius. We reveal that this modifier is homologous to the eukaryotic ubiquitin-related modifier Urm1, considered to be a close evolutionary relative of the progenitor of all ubiquitin-like proteins. Furthermore we demonstrate that urmylated substrates are recognized and processed by the archaeal proteasome, by virtue of a direct interaction with the modifier. Thus, the regulation of protein stability by Urm1 and the proteasome in archaea is likely representative of an ancient pathway from which eukaryotic ubiquitin-mediated proteolysis has evolved. Nature Pub. Group 2015-09-08 /pmc/articles/PMC4569737/ /pubmed/26348592 http://dx.doi.org/10.1038/ncomms9163 Text en Copyright © 2015, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Anjum, Rana S. Bray, Sian M. Blackwood, John K. Kilkenny, Mairi L. Coelho, Matthew A. Foster, Benjamin M. Li, Shurong Howard, Julie A. Pellegrini, Luca Albers, Sonja-Verena Deery, Michael J. Robinson, Nicholas P. Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius |
title | Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius |
title_full | Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius |
title_fullStr | Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius |
title_full_unstemmed | Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius |
title_short | Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius |
title_sort | involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon sulfolobus acidocaldarius |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4569737/ https://www.ncbi.nlm.nih.gov/pubmed/26348592 http://dx.doi.org/10.1038/ncomms9163 |
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