Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy

Eri Sakata, Stefan Bohn, Oana Mihalache, Petra Kiss, Florian Beck, Istvan Nagy, Stephan Nickell, Keiji Tanaka, Yasushi Saeki, Friedrich Förster, Wolfgang Baumeister

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Two canonical subunits of the 26S proteasome, Rpn10 and Rpn13, function as ubiquitin (Ub) receptors. The mutual arrangement of these subunits--and all other non-ATPase subunits--in the regulatory particle is unknown. Using electron cryomicroscopy, we calculated difference maps between wild-type 26S proteasome from Saccharomyces cerevisiae and deletion mutants (rpn10Δ, rpn13Δ, and rpn10Δrpn13Δ). These maps allowed us to localize the two Ub receptors unambiguously. Rpn10 and Rpn13 mapped to the apical part of the 26S proteasome, above the N-terminal coiled coils of the AAA-ATPase heterodimers Rpt4/Rpt5 and Rpt1/Rpt2, respectively. On the basis of the mutual positions of Rpn10 and Rpn13, we propose a model for polyubiquitin binding to the 26S proteasome.

Original languageEnglish
Pages (from-to)1479-84
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume109
Issue number5
DOIs
Publication statusPublished - 31 Jan 2012
Externally publishedYes

Keywords

  • Animals
  • Cryoelectron Microscopy
  • Drosophila melanogaster
  • Mass Spectrometry
  • Models, Molecular
  • Proteasome Endopeptidase Complex
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins

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