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

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  • Rana S. Anjum
  • Sian M. Bray
  • John K. Blackwood
  • Mairi L. Kilkenny
  • Matthew A. Coelho
  • Benjamin M. Foster
  • Shurong Li
  • Julie A. Howard
  • Luca Pellegrini
  • Sonja-Verena Albers
  • Michael J. Deery
  • Nicholas P. Robinson
Article number8163
<mark>Journal publication date</mark>8/09/2015
<mark>Journal</mark>Nature Communications
Number of pages15
Publication StatusPublished
<mark>Original language</mark>English


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.