Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius

Anjum, Rana S. and Bray, Sian M. and Blackwood, John K. and Kilkenny, Mairi L. and Coelho, Matthew A. and Foster, Benjamin M. and Li, Shurong and Howard, Julie A. and Pellegrini, Luca and Albers, Sonja-Verena and Deery, Michael J. and Robinson, Nicholas P. (2015) Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius. Nature Communications, 6. ISSN 2041-1723

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Abstract

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.

Item Type: Journal Article
Journal or Publication Title: Nature Communications
Uncontrolled Keywords: /dk/atira/pure/subjectarea/asjc/3100
Subjects:
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 86207
Deposited By: ep_importer_pure
Deposited On: 04 May 2017 13:24
Refereed?: Yes
Published?: Published
Last Modified: 11 Feb 2020 03:24
URI: https://eprints.lancs.ac.uk/id/eprint/86207

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