Abstract
The 26S proteasome is thought to be a homogenous complex, consisting of a 20S proteolytic core and a 19S regulatory particle that is required for its activation. Two groups have recently reported the activation of archeal 20S by a p97-related double-ring AAA+ ATPase complex, in a similar fashion to that reported for 19S. Since p97 is found in eukaryotes, the existence of a parallel setting in higher organisms is intriguing. Herein, we present supporting data and hypothesize that in eukaryotes, p97 and CSN form a promiscuous, hence hard-to-detect, "alternative cap", enabling the prompt and precise elimination of particular substrates.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Archaeal Proteins / chemistry
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Archaeal Proteins / genetics
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Archaeal Proteins / physiology*
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Endopeptidases / chemistry
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Endopeptidases / genetics
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Endopeptidases / physiology*
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Evolution, Molecular
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Humans
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Methanosarcina / enzymology
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Models, Molecular
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Proteasome Endopeptidase Complex / chemistry
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Proteasome Endopeptidase Complex / genetics
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Proteasome Endopeptidase Complex / physiology*
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Protein Multimerization
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Protein Structure, Quaternary
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Protein Subunits / chemistry
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Protein Subunits / genetics
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Protein Subunits / physiology
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Thermoplasma / enzymology
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Ubiquitination
Substances
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Archaeal Proteins
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Protein Subunits
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Endopeptidases
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Proteasome Endopeptidase Complex
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ATP dependent 26S protease
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proteasome, Thermoplasma