ArticlePLoS genetics2018
The Hsp70 co-chaperone Ydj1/HDJ2 regulates ribonucleotide reductase activity.
Article in PLoS genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 35 citations in OpenAlex.
- Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response.Nature communications · 2025Article
- Inhibition of the assembly ofmBio · 2025Article
- E2 ubiquitin-conjugating enzyme Ubc11 regulates Rst2 protein stability in the fission yeast Schizosaccharomyces pombe.Archives of microbiology · 2025Article
- Global profiling of protein complex dynamics with an experimental library of protein interaction markers.Nature biotechnology · 2025Article
- Essential role for PfHSP40 in asexual replication and thermotolerance of malaria parasites.PLoS pathogens · 2025Article
- Acetylation of the yeast Hsp40 chaperone protein Ydj1 fine-tunes proteostasis and translational fidelity.PLoS genetics · 2024Article
- Acetylation of the yeast Hsp40 chaperone protein Ydj1 fine-tunes proteostasis and translational fidelity.bioRxiv : the preprint server for biology · 2024Article
- Synergistic Effect of a Combination of Proteasome and Ribonucleotide Reductase Inhibitors in a Biochemical Model of the YeastInternational journal of molecular sciences · 2024Article
- Novel insights into the post-translational modifications of Ydj1/DNAJA1 co-chaperones.Cell stress & chaperones · 2024Review
- DNAJA2 deficiency activates cGAS-STING pathway via the induction of aberrant mitosis and chromosome instability.Nature communications · 2023Article
- Molecular Chaperones' Potential against Defective Proteostasis of Amyotrophic Lateral Sclerosis.Cells · 2023Review
- Yeast Ribonucleotide Reductase Is a Direct Target of the Proteasome and Provides Hyper Resistance to the Carcinogen 4-NQO.Journal of fungi (Basel, Switzerland) · 2023Article
- Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.PLoS biology · 2022Article
- The APE2 Exonuclease Is a Client of the Hsp70-Hsp90 Axis in Yeast and Mammalian Cells.Biomolecules · 2022Article
- The HSP40 chaperone Ydj1 drives amyloid beta 42 toxicity.EMBO molecular medicine · 2022Article
- The C-terminal domain of Hsp70 is responsible for paralog-specific regulation of ribonucleotide reductase.PLoS genetics · 2022Article
- Role of Biomarkers in FLT3 AML.Cancers · 2022Review
- Chemogenomic and bioinformatic profiling of ERdj paralogs underpins their unique roles in cancer.Cell stress & chaperones · 2021Article
- Chemogenomic screening identifies the Hsp70 co-chaperone DNAJA1 as a hub for anticancer drug resistance.Scientific reports · 2020Article
- The Yeast Hsp70 Cochaperone Ydj1 Regulates Functional Distinction of Ssa Hsp70s in the Hsp90 Chaperoning Pathway.Genetics · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Hsp70 is a well-conserved molecular chaperone involved in the folding, stabilization, and eventual degradation of many "client" proteins. Hsp70 is regulated by a suite of co-chaperone molecules that assist in Hsp70-client interaction and stimulate the intrinsic ATPase activity of Hsp70. While previous studies have shown the anticancer target ribonucleotide reductase (RNR) is a client of Hsp70, the regulatory co-chaperones involved remain to be determined. To identify co-chaperone(s) involved in RNR activity, 28 yeast co-chaperone knockout mutants were screened for sensitivity to the RNR-perturbing agent Hydroxyurea. Ydj1, an important cytoplasmic Hsp70 co-chaperone was identified to be required for growth on HU. Ydj1 bound the RNR subunit Rnr2 and cells lacking Ydj1 showed a destabilized RNR complex. Suggesting broad conservation from yeast to human, HDJ2 binds R2B and regulates RNR stability in human cells. Perturbation of the Ssa1-Ydj1 interaction through mutation or Hsp70-HDJ2 via the small molecule 116-9e compromised RNR function, suggesting chaperone dependence of this novel role. Mammalian cells lacking HDJ2 were significantly more sensitive to RNR inhibiting drugs such as hydroxyurea, gemcitabine and triapine. Taken together, this work suggests a novel anticancer strategy-inhibition of RNR by targeting Hsp70 co-chaperone function.
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