Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 5, Pages 1479-1484Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1119394109
Keywords
EM single-particle analysis; protein degradation; ubiquitin-proteasome pathway; subunit localization; quantitative mass spectrometry
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Funding
- Max-Planck Society
- European Union [HEALTH-F4-2008-201648]
- Deutsche Forschungsgemeinschaft [SFB 594]
- Human Frontier Science Project
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Targeted Research Program
- Grants-in-Aid for Scientific Research [24657097] Funding Source: KAKEN
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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 (rpn10 Delta, rpn13 Delta, and rpn10 Delta rpn13 Delta). 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.
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