ArticleMolecular biology of the cell2003
Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+].
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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79 citing papers in PubMed, 121 citations in OpenAlex.
- Comparative structural and functional analysis of the glycine-rich regions of Class A and B J-domain protein cochaperones of Hsp70.FEBS letters · 2024Article
- Mrj is a chaperone of the Hsp40 family that regulates Orb2 oligomerization and long-term memory in Drosophila.PLoS biology · 2024Article
- Unique characteristics of the J-domain proximal regions of Hsp70 cochaperone Apj1 in prion propagation/elimination and its overlap with Sis1 function.Frontiers in molecular biosciences · 2024Article
- Identification of subfunctionalized aggregate-remodeling J-domain proteins in Arabidopsis thaliana.Journal of experimental botany · 2023Article
- Human J-Domain Protein DnaJB6 Protects Yeast from [Biology · 2022Article
- Article
- Review
- Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors.Nature communications · 2022Article
- Essentiality of Sis1, a J-domain protein Hsp70 cochaperone, can be overcome by Tti1, a specialized PIKK chaperone.Molecular biology of the cell · 2022Article
- Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein.Genetics · 2021Article
- Sis1 potentiates the stress response to protein aggregation and elevated temperature.Nature communications · 2020Article
- Chaperoning of asparagine repeat-containing proteins inJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2020Review
- Inhibition of DNAJ-HSP70 interaction improves strength in muscular dystrophy.The Journal of clinical investigation · 2020Article
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- Three J-proteins impact Hsp104-mediated variant-specific prion elimination: a new critical role for a low-complexity domain.Current genetics · 2020Review
- Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain.PloS one · 2020Article
- Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.The Biochemical journal · 2019Review
- Co-evolution of spliceosomal disassembly interologs: crowning J-protein component with moonlighting RNA-binding activity.Current genetics · 2019Article
- Molecular dynamics simulations of Hsp40 J-domain mutants identifies disruption of the critical HPD-motif as the key factor for impaired curing in vivo of the yeast prion [URE3].Journal of biomolecular structure & dynamics · 2018Article
19 more citing papers are in PubMed but not listed here.
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3 authors at 1 institution in 1 country.
Funding
Abstract
Sis1 and Ydj1, functionally distinct heat shock protein (Hsp)40 molecular chaperones of the yeast cytosol, are homologs of Hdj1 and Hdj2 of mammalian cells, respectively. Sis1 is necessary for propagation of the Saccharomyces cerevisiae prion [RNQ(+)]; Ydj1 is not. The ability to function in [RNQ(+)] maintenance has been conserved, because Hdj1 can function to maintain Rnq1 in an aggregated form in place of Sis1, but Hdj2 cannot. An extended glycine-rich region of Sis1, composed of a region rich in phenylalanine residues (G/F) and another rich in methionine residues (G/M), is critical for prion maintenance. Single amino acid alterations in a short stretch of amino acids of the G/F region of Sis1 that are absent in the otherwise highly conserved G/F region of Ydj1 cause defects in prion maintenance. However, there is some functional redundancy within the glycine-rich regions of Sis1, because a deletion of the adjacent glycine/methionine (G/M) region was somewhat defective in propagation of [RNQ(+)] as well. These results are consistent with a model in which the glycine-rich regions of Hsp40s contain specific determinants of function manifested through interaction with Hsp70s.
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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.