ArticleProceedings of the National Academy of Sciences of the United States of America1998
Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digests of enolase 1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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Who cites it
88 citing papers in PubMed.
- Proteasome-derived peptides: separating the trash from the recycling.Trends in biochemical sciences · 2025Review
- An mRNA Vaccine for Herpes Zoster and Its Efficacy Evaluation in Naïve/Primed Murine Models.Vaccines · 2025Article
- Stimulation of the immune system by a tumor antigen-bearing adenovirus-inspired VLP allows control of melanoma growth.Molecular therapy. Methods & clinical development · 2023Article
- Decoding the secrets: how conformational and structural regulators inhibit the human 20S proteasome.Frontiers in chemistry · 2023Article
- Isolation of Proteasome-Trapped Peptides (PTPs) for Degradome Analysis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Proteasome inhibitors in medullary thyroid carcinoma: time to restart with clinical trials?Frontiers in endocrinology · 2023Review
- Adenovirus-Inspired Virus-Like-Particles Displaying Melanoma Tumor Antigen Specifically Target Human DC Subsets and Trigger Antigen-Specific Immune Responses.Biomedicines · 2022Article
- Peptidomimetics Based onBiomolecules · 2022Article
- The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag.Nature communications · 2021Article
- The role of tumor necrosis factor-α and interferon-γ in the hyperglycemia-induced ubiquitination and loss of platelet endothelial cell adhesion molecule-1 in rat retinal endothelial cells.Microcirculation (New York, N.Y. : 1994) · 2021Article
- Structural Insights into Substrate Recognition and Processing by the 20S Proteasome.Biomolecules · 2021Review
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Joint epitope selection and spacer design for string-of-beads vaccines.Bioinformatics (Oxford, England) · 2020Article
- Immunoinformatics: Predicting Peptide-MHC Binding.Annual review of biomedical data science · 2020Article
- Tumors escape immunosurveillance by overexpressing the proteasome activator PSME3.Oncoimmunology · 2020Article
- Measles Vaccines Designed for Enhanced CD8Viruses · 2020Article
- Targeting Protein Kinase G to Treat Cardiac Proteotoxicity.Frontiers in physiology · 2020Review
- Crystal structure of suboptimal viral fragments of Epstein Barr Virus Rta peptide-HLA complex that stimulate CD8 T cell response.Scientific reports · 2019Article
- Substrate selection by the proteasome through initiation regions.Protein science : a publication of the Protein Society · 2019Review
- Proline- and Arginine-Rich Peptides as Flexible Allosteric Modulators of Human Proteasome Activity.Journal of medicinal chemistry · 2019Article
28 more citing papers are in PubMed but not listed here.
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12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 436-amino acid protein enolase 1 from yeast was degraded in vitro by purified wild-type and mutant yeast 20S proteasome particles. Analysis of the cleavage products at different times revealed a processive degradation mechanism and a length distribution of fragments ranging from 3 to 25 amino acids with an average length of 7 to 8 amino acids. Surprisingly, the average fragment length was very similar between wild-type and mutant 20S proteasomes with reduced numbers of active sites. This implies that the fragment length is not influenced by the distance between the active sites, as previously postulated. A detailed analysis of the cleavages also allowed the identification of certain amino acid characteristics in positions flanking the cleavage site that guide the selection of the P1 residues by the three active beta subunits. Because yeast and mammalian proteasomes are highly homologous, similar cleavage motifs might be used by mammalian proteasomes. Therefore, our data provide a basis for predicting proteasomal degradation products from which peptides are sampled by major histocompatibility complex class I molecules for presentation to cytotoxic T cells.
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