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Biochem Biophys Res Commun. 2009 Oct 16;388(2):228-33. doi: 10.1016/j.bbrc.2009.07.145. Epub 2009 Aug 3.

An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome.

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  • 1Department of Structural Biology, Max-Planck-Institute of Biochemistry, D-82152 Martinsried, Germany.

Abstract

The 26S proteasome is the most downstream element of the ubiquitin-proteasome pathway of protein degradation. It is composed of the 20S core particle (CP) and the 19S regulatory particle (RP). The RP consists of 6 AAA-ATPases and at least 13 non-ATPase subunits. Based on a cryo-EM map of the 26S proteasome, structures of homologs, and physical protein-protein interactions we derive an atomic model of the AAA-ATPase-CP sub-complex. The ATPase order in our model (Rpt1/Rpt2/Rpt6/Rpt3/Rpt4/Rpt5) is in excellent agreement with the recently identified base-precursor complexes formed during the assembly of the RP. Furthermore, the atomic CP-AAA-ATPase model suggests that the assembly chaperone Nas6 facilitates CP-RP association by enhancing the shape complementarity between Rpt3 and its binding CP alpha subunits partners.

PMID:
19653995
[PubMed - indexed for MEDLINE]
PMCID:
PMC2771176
Free PMC Article
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