ArticlePloS one2012
The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 17 citations in OpenAlex.
- Nematode CDC-37 and DNJ-13 form complexes and can interact with HSP-90.Scientific reports · 2021Article
- Comparative analysis of the coordinated motion of Hsp70s from different organelles observed by single-molecule three-color FRET.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Proteostasis collapse is a driver of cell aging and death.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- head-bent resistant Hsc70 variants show reduced Hsp40 affinity and altered protein folding activity.Scientific reports · 2019Article
- Dual Role of Ribosome-Binding Domain of NAC as a Potent Suppressor of Protein Aggregation and Aging-Related Proteinopathies.Molecular cell · 2019Article
- Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding.Molecular & cellular proteomics : MCP · 2019Article
- Two-Dimensional Gel Electrophoresis-Based Proteomic Analysis Reveals N-terminal Truncation of the Hsc70 Protein in Cotton Fibers In Vivo.Scientific reports · 2016Article
- Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.Molecular & cellular proteomics : MCP · 2016Article
- Selective activators of protein phosphatase 5 target the auto-inhibitory mechanism.Bioscience reports · 2015Article
- The balanced regulation of Hsc70 by DNJ-13 and UNC-23 is required for muscle functionality.The Journal of biological chemistry · 2014Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsc70 is a conserved ATP-dependent molecular chaperone, which utilizes the energy of ATP hydrolysis to alter the folding state of its client proteins. In contrast to the Hsc70 systems of bacteria, yeast and humans, the Hsc70 system of C. elegans (CeHsc70) has not been studied to date.We find that CeHsc70 is characterized by a high ATP turnover rate and limited by post-hydrolysis nucleotide exchange. This rate-limiting step is defined by the helical lid domain at the C-terminus. A certain truncation in this domain (CeHsc70-Δ545) reduces the turnover rate and renders the hydrolysis step rate-limiting. The helical lid domain also affects cofactor affinities as the lidless mutant CeHsc70-Δ512 binds more strongly to DNJ-13, forming large protein complexes in the presence of ATP. Despite preserving the ability to hydrolyze ATP and interact with its cofactors DNJ-13 and BAG-1, the truncation of the helical lid domain leads to the loss of all protein folding activity, highlighting the requirement of this domain for the functionality of the nematode's Hsc70 protein.
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