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

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 and Nicholas P. Robinson ()
Additional contact information
Rana S. Anjum: University of Cambridge
Sian M. Bray: University of Cambridge
John K. Blackwood: University of Cambridge
Mairi L. Kilkenny: University of Cambridge
Matthew A. Coelho: University of Cambridge
Benjamin M. Foster: University of Cambridge
Shurong Li: University of Cambridge
Julie A. Howard: Cambridge Centre for Proteomics
Luca Pellegrini: University of Cambridge
Sonja-Verena Albers: Molecular Biology of Archaea, Max Planck Institute for Terrestrial Microbiology
Michael J. Deery: Cambridge Centre for Proteomics
Nicholas P. Robinson: University of Cambridge

Nature Communications, 2015, vol. 6, issue 1, 1-15

Abstract: 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.

Date: 2015
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms9163 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9163

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms9163

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().