ArticlePloS one2011
Expression of a malarial Hsp70 improves defects in chaperone-dependent activities in ssa1 mutant yeast.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- The Role of Hsp70s in the Development and Pathogenicity of Plasmodium falciparum.Advances in experimental medicine and biology · 2021Article
- Role of the J Domain Protein Family in the Survival and Pathogenesis of Plasmodium falciparum.Advances in experimental medicine and biology · 2021Review
- Comparative Characterization ofBiomolecules · 2020Article
- Small Molecule Inhibitors Targeting the Heat Shock Protein System of Human Obligate Protozoan Parasites.International journal of molecular sciences · 2019Review
- Exploring Novel Functions of the Small GTPase Ypt1p under Heat-Shock by Characterizing a Temperature-Sensitive Mutant Yeast Strain,International journal of molecular sciences · 2019Article
- A mitochondrial HSP70 (HSPA9B) is linked to miltefosine resistance and stress response in Leishmania donovani.Parasites & vectors · 2016Article
- Article
- Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.Journal of molecular biology · 2015Article
- Article
- Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle.Frontiers in molecular biosciences · 2015Review
- Expression profiling of Plasmodium berghei HSP70 genes for generation of bright red fluorescent parasites.PloS one · 2013Article
- The endoplasmic reticulum-associated degradation pathways of budding yeast.Cold Spring Harbor perspectives in biology · 2012Review
- Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Microbiology and molecular biology reviews : MMBR · 2012Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Plasmodium falciparum causes the most virulent form of malaria and encodes a large number of molecular chaperones. Because the parasite encounters radically different environments during its lifecycle, many members of this chaperone ensemble may be essential for P. falciparum survival. Therefore, Plasmodium chaperones represent novel therapeutic targets, but to establish the mechanism of action of any developed therapeutics, it is critical to ascertain the functions of these chaperones. To this end, we report the development of a yeast expression system for PfHsp70-1, a P. falciparum cytoplasmic chaperone. We found that PfHsp70-1 repairs mutant growth phenotypes in yeast strains lacking the two primary cytosolic Hsp70s, SSA1 and SSA2, and in strains harboring a temperature sensitive SSA1 allele. PfHsp70-1 also supported chaperone-dependent processes such as protein translocation and ER associated degradation, and ameliorated the toxic effects of oxidative stress. By introducing engineered forms of PfHsp70-1 into the mutant strains, we discovered that rescue requires PfHsp70-1 ATPase activity. Together, we conclude that yeast can be co-opted to rapidly uncover specific cellular activities mediated by malarial chaperones.
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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.