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Title

Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29

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Published in Molecular and Cellular Biology. 2011, vol. 31, no. 8, p. 1610-23
Abstract In this study we determine that the Not4 E3 ligase is important for proteasome integrity. Consequently, deletion of Not4 leads to an accumulation of polyubiquitinated proteins and reduced levels of free ubiquitin. In the absence of Not4, the proteasome regulatory particle (RP) and core particle (CP) form salt-resistant complexes, and all other forms of RPs are unstable. Not4 can associate with RP species present in purified proteasome holoenzyme but not with purified RP. Additionally, Not4 interacts with Ecm29, a protein that stabilizes the proteasome. Interestingly, Ecm29 is identified in RP species that are inactive and not detectable in cells lacking Not4. In the absence of Not4, Ecm29 interacts less well with the proteasome and becomes ubiquitinated and degraded. Our results characterize Ecm29 as a proteasome chaperone whose appropriate interaction with the proteasome requires Not4.
Keywords Holoenzymes/metabolismHomeostasisProteasome Endopeptidase Complex/genetics/metabolismProtein BindingSaccharomyces cerevisiae/genetics/metabolismSaccharomyces cerevisiae Proteins/genetics/metabolismUbiquitin/metabolismUbiquitin-Protein Ligases/deficiency/genetics/metabolism
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PMID: 21321079
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Article (Published version) (1.7 MB) - document accessible for UNIGE members only Limited access to UNIGE
Structures
Research group Groupe Collart Martine (microbiologie et médecine moléculaire) (81)
Project FNS: 3100AO-100793
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PANASENKO, Olesya, COLLART, Martine. Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29. In: Molecular and Cellular Biology, 2011, vol. 31, n° 8, p. 1610-23. https://archive-ouverte.unige.ch/unige:30084

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Deposited on : 2013-10-01

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