ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences1999
The 26S proteasome of the fission yeast Schizosaccharomyces pombe.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Proteasome regulation of petite-negativity in fission yeast.BMC biology · 2025Article
- Integrative analysis of Hub1 overexpression: driving transcriptional reprogramming and alternative splicing in Saccharomyces cerevisiae.BMC genomics · 2025Article
- Quality control mechanisms that protect nuclear envelope identity and function.The Journal of cell biology · 2022Review
- The Protein Level of Rev1, a TLS Polymerase in Fission Yeast, Is Strictly Regulated during the Cell Cycle and after DNA Damage.PloS one · 2015Article
- Implications for proteasome nuclear localization revealed by the structure of the nuclear proteasome tether protein Cut8.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Article
- A Cds1-mediated checkpoint protects the MBF activator Rep2 from ubiquitination by anaphase-promoting complex/cyclosome-Ste9 at S-phase arrest in fission yeast.Molecular and cellular biology · 2009Article
- Fission yeast Dss1 associates with the proteasome and is required for efficient ubiquitin-dependent proteolysis.The Biochemical journal · 2006Article
- The RPN1 subunit of the 26S proteasome in Arabidopsis is essential for embryogenesis.The Plant cell · 2005Article
- Use of RNA interference and complementation to study the function of the Drosophila and human 26S proteasome subunit S13.Molecular and cellular biology · 2003Article
- Sum1, a component of the fission yeast eIF3 translation initiation complex, is rapidly relocalized during environmental stress and interacts with components of the 26S proteasome.Molecular biology of the cell · 2002Article
- Relating whole-genome expression data with protein-protein interactions.Genome research · 2002Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The 26S proteasome is the multiprotein complex that degrades proteins that have been marked for destruction by the ubiquitin pathway. It is made up of two multisubunit complexes, the 20S catalytic core and the 19S regulatory complex. We describe the isolation and characterization of conditional mutants in the regulatory complex and their use to investigate interactions between different subunits. In addition we have investigated the localization of the 26S proteasome in fission yeast, by immunofluorescence in fixed cells and live cells with the use of a GFP-tagged subunit. Surprisingly, we find that in mitotic cells the 26S proteasome occupies a discrete intracellular compartment, the nuclear periphery. Electron microscopic analysis demonstrates that the complex resides inside the nuclear envelope. During meiosis the localization showed a more dynamic distribution. In meiosis I the proteasome remained around the nuclear periphery. However, during meiosis II there was a dramatic relocalization: initially, the signal occupied the area between the dividing nuclei, but at the end of mitosis the signal dispersed, returning to the nuclear periphery on ascospore formation. This observation implies that the nuclear periphery is a major site of proteolysis in yeast during mitotic growth and raises important questions about the function of the 26S proteasome in protein degradation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.