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

Friedrich Förster, Keren Lasker, Florian Beck, Stephan Nickell, Andrej Sali, Wolfgang Baumeister

Research output: Contribution to journalArticleAcademicpeer-review

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.

Original languageEnglish
Pages (from-to)228-33
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume388
Issue number2
DOIs
Publication statusPublished - 2009
Externally publishedYes

Keywords

  • Adenosine Triphosphatases
  • Animals
  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Drosophila melanogaster
  • Proteasome Endopeptidase Complex
  • Protein Structure, Quaternary

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