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- Title
Evolution of Proteasome Regulators in Eukaryotes.
- Authors
Fort, Philippe; Kajava, Andrey V.; Delsuc, Fredéric; Coux, Olivier
- Abstract
All living organisms require protein degradation to terminate biological processes and remove damaged proteins. One suchmachine is the 20S proteasome, a specialized barrel-shaped and compartmentalized multicatalytic protease. The activity of the 20S proteasome generally requires the binding of regulators/proteasome activators (PAs), which control the entrance of substrates. These include the PA700 (19Scomplex),which assembles with the 20S and forms the 26S proteasome and allows the efficient degradation of proteins usually labeled by ubiquitin tags, PA200 and PA28, which are involved in proteolysis through ubiquitin-independent mechanisms and PI31, which was initially identified as a 20S inhibitor in vitro. Unlike 20S proteasome, shown to be present in all Eukaryotes and Archaea, the evolutionary history of PAs remained fragmentary. Here, we made a comprehensive survey and phylogenetic analyses of the four types of regulators in 17 clades coveringmost of the eukaryotic supergroups. We found remarkable conservation of each PA700 subunit in all eukaryotes, indicating that the current complex PA700 structurewas already set up in the last eukaryotic common ancestor (LECA). Also present in LECA, PA200, PA28, and PI31 showed a more contrasted evolutionary picture, becausemany lineages have subsequently lost one or twoof them. The paramount conservation of PA700 composition in all eukaryotes and the dynamic evolutionof PA200, PA28, and PI31 are discussed inthe light of current knowledge on their physiological roles.
- Subjects
PROTEASOMES; UBIQUITIN; BIOLOGICAL evolution; EUKARYOTIC cells; MULTICELLULAR organisms
- Publication
Genome Biology & Evolution, 2015, Vol 7, Issue 5, p1363
- ISSN
1759-6653
- Publication type
Article
- DOI
10.1093/gbe/evv068