ArticleThe Journal of cell biology2012
Biogenesis of the mitochondrial Hsp70 chaperone.
Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Review
- A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Redox Aspects of Chaperones in Cardiac Function.Frontiers in physiology · 2018Review
- Time, space, and disorder in the expanding proteome universe.Proteomics · 2017Article
- Mitochondrial heat shock protein (Hsp) 70 and Hsp10 cooperate in the formation of Hsp60 complexes.The Journal of biological chemistry · 2015Article
- Article
- Gene therapy with mitochondrial heat shock protein 70 suppresses visual loss and optic atrophy in experimental autoimmune encephalomyelitis.Investigative ophthalmology & visual science · 2014Article
- The functional interaction of mitochondrial Hsp70s with the escort protein Zim17 is critical for Fe/S biogenesis and substrate interaction at the inner membrane preprotein translocase.The Journal of biological chemistry · 2013Article
- Real-time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET.The EMBO journal · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperones mediate protein folding and prevent deleterious protein aggregation in the cell. However, little is known about the biogenesis of chaperones themselves. In this study, we report on the biogenesis of the yeast mitochondrial Hsp70 (mtHsp70) chaperone, which is essential for the functionality of mitochondria. We show in vivo and in organello that mtHsp70 rapidly folds after its import into mitochondria, with its ATPase domain and peptide-binding domain (PBD) adopting their structures independently of each other. Importantly, folding of the ATPase domain but not of the PBD was severely affected in the absence of the Hsp70 escort protein, Hep1. We reconstituted the folding of mtHsp70, demonstrating that Hep1 and ATP/ADP were required and sufficient for its de novo folding. Our data show that Hep1 bound to a folding intermediate of mtHsp70. Binding of an adenine nucleotide triggered release of Hep1 and folding of the intermediate into native mtHsp70. Thus, Hep1 acts as a specialized chaperone mediating the de novo folding of an Hsp70 chaperone.
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Registered trials
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