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 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.
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Rana S
RS
Anjum
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Sian M
SM
Bray
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
John K
JK
Blackwood
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Mairi L
ML
Kilkenny
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Matthew A
MA
Coelho
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Benjamin M
BM
Foster
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Shurong
S
Li
Department of Biochemistry and Cambridge Systems Biology Centre, Cambridge Centre for Proteomics, Cambridge CB2 1QR, UK.
Julie A
JA
Howard
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Luca
L
Pellegrini
Molecular Biology of Archaea, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.
Sonja-Verena
SV
Albers
Department of Biochemistry and Cambridge Systems Biology Centre, Cambridge Centre for Proteomics, Cambridge CB2 1QR, UK.
Michael J
MJ
Deery
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Nicholas P
NP
Robinson
D019843:Archaeal Proteins / Q000235:genetics* / Q000378:metabolism; D002850:Chromatography, Gel; D002853:Chromatography, Liquid; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D013058:Mass Spectrometry; D008854:Microscopy, Electron; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism* / Q000648:ultrastructure; D059748:Proteolysis; D016945:Sulfolobus acidocaldarius / Q000235:genetics* / Q000378:metabolism; D014452:Ubiquitins / Q000235:genetics* / Q000378:metabolism
D019843:Archaeal Proteins; D014452:Ubiquitins; D046988:Proteasome Endopeptidase Complex