ArticleBMC developmental biology2008
C. elegans dss-1 is functionally conserved and required for oogenesis and larval growth.
Article in BMC developmental biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 39 citations in OpenAlex.
- A novel endoplasmic reticulum adaptation is critical for the long-lived Caenorhabditis elegans rpn-10 proteasomal mutant.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Article
- CRISPR/Cas9-Targeted Disruption of Two Highly HomologousInternational journal of molecular sciences · 2023Article
- An antisteatosis response regulated by oleic acid through lipid droplet-mediated ERAD enhancement.Science advances · 2023Article
- BRCA2-DSS1 interaction is dispensable for RAD51 recruitment at replication-induced and meiotic DNA double strand breaks.Nature communications · 2022Article
- Proteolysis in Reproduction: Lessons From Gene-Modified Organism Studies.Frontiers in endocrinology · 2022Review
- Proteasomal subunit depletions differentially affect germline integrity inFrontiers in cell and developmental biology · 2022Article
- THSC/TREX-2 deficiency causes replication stress and genome instability in Caenorhabditis elegans.Journal of cell science · 2021Article
- Intrinsically disordered protein AtDSS1(V) participates in plant defense response to oxidative stress.Protoplasma · 2021Article
- The conserved multi-functional nuclear proteinmicroPublication biology · 2020Article
- Loss of proteasome subunit RPN-12 causes an increased mean lifespan at a higher temperature inmicroPublication biology · 2020Article
- Sem1 links proteasome stability and specificity to multicellular development.PLoS genetics · 2018Article
- Resveratrol reduces amyloid-beta (Aβ₁₋₄₂)-induced paralysis through targeting proteostasis in an Alzheimer model of Caenorhabditis elegans.European journal of nutrition · 2016Article
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- Promotion of BRCA2-Dependent Homologous Recombination by DSS1 via RPA Targeting and DNA Mimicry.Molecular cell · 2015Article
- Effects of plant extracts on the reversal of glucose-induced impairment of stress-resistance in Caenorhabditis elegans.Plant foods for human nutrition (Dordrecht, Netherlands) · 2014Article
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- Specific SKN-1/Nrf stress responses to perturbations in translation elongation and proteasome activity.PLoS genetics · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundDss1 (or Rpn15) is a recently identified subunit of the 26S proteasome regulatory particle. In addition to its function in the protein degradation machinery, it has been linked to BRCA2 (breast cancer susceptibility gene 2 product) and homologous DNA recombination, mRNA export, and exocytosis. While the fungal orthologues of Dss1 are not essential for viability, the significance of Dss1 in metazoans has remained unknown due to a lack of knockout animal models.
resultsIn the current study deletion of dss-1 was studied in Caenorhabditis elegans with a dss-1 loss-of-function mutant and dss-1 directed RNAi. The analysis revealed an essential role for dss-1 in oogenesis. In addition, dss-1 RNAi caused embryonic lethality and larval arrest, presumably due to loss of the dss-1 mRNA maternal contribution. DSS-1::GFP fusion protein localised primarily in the nucleus. No apparent effect on proteasome function was found in dss-1 RNAi treated worms. However, expression of the C. elegans dss-1 in yeast cells deleted for its orthologue SEM1 rescued their temperature-sensitive growth phenotype, and partially rescued the accumulation of polyubiquitinated proteins in these cells.
conclusionThe first knockout animal model for the gene encoding the proteasome subunit DSS-1/Rpn15/Sem1 is characterised in this study. In contrast to unicellular eukaryotes, the C. elegans dss-1 encodes an essential protein, which is required for embryogenesis, larval growth, and oogenesis, and which is functionally conserved with its yeast and human homologues.
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