ArticleThe Journal of biological chemistry2016
Distinct Elements in the Proteasomal β5 Subunit Propeptide Required for Autocatalytic Processing and Proteasome Assembly.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 23 citations in OpenAlex.
- Molecular basis for the stepwise and faithful maturation of the 20Science advances · 2025Article
- PSMG2 role in tumorigenesis and stemness mediated by protein accumulation, reticulum stress and autophagy.International journal of biological sciences · 2025Article
- Structural roles of Ump1 and β-subunit propeptides in proteasome biogenesis.Life science alliance · 2024Article
- Structural basis of human 20S proteasome biogenesis.Nature communications · 2024Article
- Mechanism of autocatalytic activation during proteasome assembly.Nature structural & molecular biology · 2024Article
- Review
- Chaperone-mediated assembly of the proteasome core particle - recent developments and structural insights.Journal of cell science · 2022Review
- Interaction with the Assembly Chaperone Ump1 Promotes Incorporation of the β7 Subunit into Half-Proteasome Precursor Complexes Driving Their Dimerization.Biomolecules · 2022Article
- Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Cooperativity in Proteasome Core Particle Maturation.iScience · 2020Article
- Proteasome β5 subunit overexpression improves proteostasis during aging and extends lifespan in Drosophila melanogaster.Scientific reports · 2019Article
- Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation.Frontiers in molecular biosciences · 2019Review
- Regulation of proteasome assembly and activity in health and disease.Nature reviews. Molecular cell biology · 2018Review
- Proteasome Structure and Assembly.Journal of molecular biology · 2017Review
- A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome.Nature communications · 2016Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Eukaryotic 20S proteasome assembly remains poorly understood. The subunits stack into four heteroheptameric rings; three inner-ring subunits (β1, β2, and β5) bear the protease catalytic residues and are synthesized with N-terminal propeptides. These propeptides are removed autocatalytically late in assembly. In Saccharomyces cerevisiae, β5 (Doa3/Pre2) has a 75-residue propeptide, β5pro, that is essential for proteasome assembly and can work in trans. We show that deletion of the poorly conserved N-terminal half of the β5 propeptide nonetheless causes substantial defects in proteasome maturation. Sequences closer to the cleavage site have critical but redundant roles in both assembly and self-cleavage. A conserved histidine two residues upstream of the autocleavage site strongly promotes processing. Surprisingly, although β5pro is functionally linked to the Ump1 assembly factor, trans-expressed β5pro associates only weakly with Ump1-containing precursors. Several genes were identified as dosage suppressors of trans-expressed β5pro mutants; the strongest encoded the β7 proteasome subunit. Previous data suggested that β7 and β5pro have overlapping roles in bringing together two half-proteasomes, but the timing of β7 addition relative to half-mer joining was unclear. Here we report conditions where dimerization lags behind β7 incorporation into the half-mer. Our results suggest that β7 insertion precedes half-mer dimerization, and the β7 tail and β5 propeptide have unequal roles in half-mer joining.
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