ArticleGenome biology and evolution2013
The complex evolutionary dynamics of Hsp70s: a genomic and functional perspective.
Article in Genome biology and evolution, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 47 citations in OpenAlex.
- Wiring of cellular proteostasis by J-domain proteins.Cell stress & chaperones · 2026Review
- Article
- Multivalent protein-protein interactions are pivotal regulators of eukaryotic Hsp70 complexes.Cell stress & chaperones · 2022Review
- Heat shock proteins and the calcineurin-crz1 signaling regulate stress responses in fungi.Archives of microbiology · 2022Review
- Interaction of client-the scaffold on which FeS clusters are build-with J-domain protein Hsc20 and its evolving Hsp70 partners.Frontiers in molecular biosciences · 2022Review
- Pathway of Hsp70 interactions at the ribosome.Nature communications · 2021Article
- Mitochondrial HSP70 Chaperone System-The Influence of Post-Translational Modifications and Involvement in Human Diseases.International journal of molecular sciences · 2021Review
- The landscape of molecular chaperones across human tissues reveals a layered architecture of core and variable chaperones.Nature communications · 2021Article
- Chaperone Networks in Fungal Pathogens of Humans.Journal of fungi (Basel, Switzerland) · 2021Review
- Structural Communication between theInternational journal of molecular sciences · 2021Article
- Computational Systems Biology of Alfalfa - Bacterial Blight Host-Pathogen Interactions: Uncovering the Complex Molecular Networks for Developing Durable Disease Resistant Crop.Frontiers in plant science · 2021Article
- The Hsp40 Mas5 Connects Protein Quality Control and the General Stress Response through the Thermo-sensitive Pyp1.iScience · 2020Article
- Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation.The Journal of biological chemistry · 2020Article
- Dynamic remodeling of the interactomes of Nematostella vectensis Hsp70 isoforms under heat shock.Journal of proteomics · 2019Article
- Genome sequence of the opportunistic human pathogen Magnusiomyces capitatus.Current genetics · 2019Article
- The Hsp70/J-protein machinery of the African trypanosome, Trypanosoma brucei.Cell stress & chaperones · 2019Article
- Oligomerization of Hsp70: Current Perspectives on Regulation and Function.Frontiers in molecular biosciences · 2019Review
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- The FKBP51 Glucocorticoid Receptor Co-Chaperone: Regulation, Function, and Implications in Health and Disease.International journal of molecular sciences · 2017Review
- How Do J-Proteins Get Hsp70 to Do So Many Different Things?Trends in biochemical sciences · 2017Review
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
Abstract
Hsp70 molecular chaperones are ubiquitous. By preventing aggregation, promoting folding, and regulating degradation, Hsp70s are major factors in the ability of cells to maintain proteostasis. Despite a wealth of functional information, little is understood about the evolutionary dynamics of Hsp70s. We undertook an analysis of Hsp70s in the fungal clade Ascomycota. Using the well-characterized 14 Hsp70s of Saccharomyces cerevisiae, we identified 491 orthologs from 53 genomes. Saccharomyces cerevisiae Hsp70s fall into seven subfamilies: four canonical-type Hsp70 chaperones (SSA, SSB, KAR, and SSC) and three atypical Hsp70s (SSE, SSZ, and LHS) that play regulatory roles, modulating the activity of canonical Hsp70 partners. Each of the 53 surveyed genomes harbored at least one member of each subfamily, and thus establishing these seven Hsp70s as units of function and evolution. Genomes of some species contained only one member of each subfamily that is only seven Hsp70s. Overall, members of each subfamily formed a monophyletic group, suggesting that each diversified from their corresponding ancestral gene present in the common ancestor of all surveyed species. However, the pattern of evolution varied across subfamilies. At one extreme, members of the SSB subfamily evolved under concerted evolution. At the other extreme, SSA and SSC subfamilies exhibited a high degree of copy number dynamics, consistent with a birth-death mode of evolution. KAR, SSE, SSZ, and LHS subfamilies evolved in a simple divergent mode with little copy number dynamics. Together, our data revealed that the evolutionary history of this highly conserved and ubiquitous protein family was surprising complex and dynamic.
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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.