Abstract
Proteasomes are the major energy-dependent proteolytic machines in the eukaryotic and archaeal domains of life. To execute protein degradation, the 20S core peptidase combines with the AAA+ ring of the 19S regulatory particle in eukarya or with the AAA+ proteasome-activating nucleotidase ring in some archaea. Here, we find that Cdc48 and 20S from the archaeon Thermoplasma acidophilum interact to form a functional proteasome. Cdc48 is an abundant and essential double-ring AAA+ molecular machine ubiquitously present in archaea, where its function has been uncertain, and in eukarya where Cdc48 participates by largely unknown mechanisms in diverse cellular processes, including multiple proteolytic pathways. Thus, proteolysis in collaboration with the 20S peptidase may represent an ancestral function of the Cdc48 family.
MeSH Terms
Adenosine Triphosphatases/chemistry,metabolism
Archaeal Proteins/metabolism
Cell Cycle Proteins/chemistry,metabolism
Evolution, Molecular
Green Fluorescent Proteins/chemistry,metabolism
Proteasome Endopeptidase Complex/chemistry,metabolism
Protein Folding
Proteolysis
Thermoplasma/enzymology
Valosin Containing Protein
Chemicals
Archaeal Proteins
Cell Cycle Proteins
Green Fluorescent Proteins
Proteasome Endopeptidase Complex
Adenosine Triphosphatases
Valosin Containing Protein
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Barthelme Dominik
Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Sauer Robert T
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