Insights Into the Molecular Architecture of the 26S Proteasome

Proc Natl Acad Sci U S A. 2009 Jul 21;106(29):11943-7. doi: 10.1073/pnas.0905081106. Epub 2009 Jul 6.

Abstract

Cryo-electron microscopy in conjunction with advanced image analysis was used to analyze the structure of the 26S proteasome and to elucidate its variable features. We have been able to outline the boundaries of the ATPase module in the "base" part of the regulatory complex that can vary in its position and orientation relative to the 20S core particle. This variation is consistent with the "wobbling" model that was previously proposed to explain the role of the regulatory complex in opening the gate in the alpha-rings of the core particle. In addition, a variable mass near the mouth of the ATPase ring has been identified as Rpn10, a multiubiquitin receptor, by correlating the electron microscopy data with quantitative mass spectrometry.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / ultrastructure
  • Animals
  • Cryoelectron Microscopy
  • Drosophila melanogaster / enzymology
  • Mass Spectrometry
  • Models, Molecular
  • Proteasome Endopeptidase Complex / chemistry*
  • Proteasome Endopeptidase Complex / ultrastructure
  • Protein Subunits / chemistry
  • Protein Transport

Substances

  • Protein Subunits
  • Proteasome Endopeptidase Complex
  • ATP dependent 26S protease
  • Adenosine Triphosphatases