ArticleBiochemistry2006
Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 114 citations in OpenAlex.
- Hsp70 diversification and repurposing across the tree of life: Lessons from the evolutionary and mechanistic trajectory of the Hsp70-Hsp110 chaperone system.The FEBS journal · 2026Review
- ATP modulates holdase activity of fungal and human 110-kilodalton heat shock proteins to promote protein folding.Protein science : a publication of the Protein Society · 2026Article
- Biochemical and biophysical characterization of Plasmodium falciparum glucose regulated protein 170.Scientific reports · 2025Article
- Early steps of protein disaggregation by Hsp70 chaperone and class B J-domain proteins are shaped by Hsp110.eLife · 2024Article
- Solid-to-liquid phase transition in the dissolution of cytosolic misfolded-protein aggregates.iScience · 2023Article
- A first-in-class inhibitor of Hsp110 molecular chaperones of pathogenic fungi.Nature communications · 2023Article
- Hsp70 and Hsp110 Chaperones Promote Early Steps of Proteasome Assembly.Biomolecules · 2022Article
- 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
- Pathway of Hsp70 interactions at the ribosome.Nature communications · 2021Article
- Purification and biochemical characterization of Msi3, an essential Hsp110 molecular chaperone in Candida albicans.Cell stress & chaperones · 2021Article
- Genome-wide imaging screen uncovers molecular determinants of arsenite-induced protein aggregation and toxicity.Journal of cell science · 2021Article
- General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021Article
- Direct involvement of Hsp70 ATP hydrolysis in Ubr1-dependent quality control.Molecular biology of the cell · 2020Article
- Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation.The Journal of biological chemistry · 2020Article
- Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.The Biochemical journal · 2019Review
- Chaperone-mediated reflux of secretory proteins to the cytosol during endoplasmic reticulum stress.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Understanding the role of glucose regulated protein 170 (GRP170) as a nucleotide exchange factor through molecular simulations.Journal of molecular graphics & modelling · 2018Article
- Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding.Biological chemistry · 2018Review
- Substrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone Sse1 is not obligate for its biological activities.Molecular biology of the cell · 2017Article
- A Chemogenomic Screening Platform Used to Identify Chemotypes Perturbing HSP90 Pathways.SLAS discovery : advancing life sciences R & D · 2017Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
SSE1 and SSE2 encode the essential yeast members of the Hsp70-related Hsp110 molecular chaperone family. Both mammalian Hsp110 and the Sse proteins functionally interact with cognate cytosolic Hsp70s as nucleotide exchange factors. We demonstrate here that Sse1 forms high-affinity (Kd approximately 10-8 M) heterodimeric complexes with both yeast Ssa and mammalian Hsp70 chaperones and that binding of ATP to Sse1 is required for binding to Hsp70s. Sse1.Hsp70 heterodimerization confers resistance to exogenously added protease, indicative of conformational changes in Sse1 resulting in a more compact structure. The nucleotide binding domains of both Sse1/2 and the Hsp70s dictate interaction specificity and are sufficient for mediating heterodimerization with no discernible contribution from the peptide binding domains. In support of a strongly conserved functional interaction between Hsp110 and Hsp70, Sse1 is shown to associate with and promote nucleotide exchange on human Hsp70. Nucleotide exchange activity by Sse1 is physiologically significant, as deletion of both SSE1 and the Ssa ATPase stimulatory protein YDJ1 is synthetically lethal. The Hsp110 family must therefore be considered an essential component of Hsp70 chaperone biology in the eukaryotic cell.
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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.