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Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination.

Abstract：

:The critical role of the ubiquitin-26S proteasome system in regulation of protein homeostasis in eukaryotes is well established. In contrast, the impact of the ubiquitin-independent proteolytic activity of proteasomes is poorly understood. Through biochemical analysis of mammalian lysates, we find that the 20S proteasome, latent in peptide hydrolysis, specifically cleaves more than 20% of all cellular proteins. Thirty intrinsic proteasome substrates (IPSs) were identified and in vitro studies of their processing revealed that cleavage occurs at disordered regions, generating stable products encompassing structured domains. The mechanism of IPS recognition is remarkably well conserved in the eukaryotic kingdom, as mammalian and yeast 20S proteasomes exhibit the same target specificity. Further, 26S proteasomes specifically recognize and cleave IPSs at similar sites, independent of ubiquitination, suggesting that disordered regions likely constitute the universal structural signal for IPS proteolysis by proteasomes. Finally, we show that proteasomes contribute to physiological regulation of IPS levels in living cells and the inactivation of ubiquitin-activating enzyme E1 does not prevent IPS degradation. Collectively, these findings suggest a significant contribution of the ubiquitin-independent proteasome degradation pathway to the regulation of protein homeostasis in eukaryotes.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Baugh JM,Viktorova EG,Pilipenko EV

doi

10.1016/j.jmb.2008.12.081

subject

Has Abstract

pub_date

2009-02-27 00:00:00

pages

814-27

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(09)00004-7

journal_volume

386

pub_type

杂志文章

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