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

Nature Communications
Rana S AnjumNicholas P Robinson

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.

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Citations

Dec 31, 2015·Cellular and Molecular Life Sciences : CMLS·B KhoshnoodC Grabbe
Jun 5, 2016·Cellular and Molecular Life Sciences : CMLS·Zhe Lyu, William B Whitman
May 16, 2019·Journal of Bacteriology·Nathaniel L Hepowit, Julie A Maupin-Furlow
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Jun 26, 2018··Xian FuJulie Maupin-Furlow

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Methods Mentioned

BETA
ubiquitination
pull-down
electrophoresis
size exclusion chromatography
size-exclusion chromatography
transmission electron microscopy
thermal shift
PCR
X-ray
electron microscopy

Software Mentioned

BLAST
Rad CFX Manager
Bio
PHYRE2
ImageQuant

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