ArticleThe Journal of biological chemistry2010
ATPase domain and interdomain linker play a key role in aggregation of mitochondrial Hsp70 chaperone Ssc1.
Article in The Journal of biological chemistry, 2010. 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, 34 citations in OpenAlex.
- Mitochondrial HSP70 Chaperone System-The Influence of Post-Translational Modifications and Involvement in Human Diseases.International journal of molecular sciences · 2021Review
- 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
- Article
- Autophagy competes for a common phosphatidylethanolamine pool with major cellular PE-consuming pathways in Saccharomyces cerevisiae.Genetics · 2015Article
- Role of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocation.Molecular biology of the cell · 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
- Biogenesis of the mitochondrial Hsp70 chaperone.The Journal of cell biology · 2012Article
- The DNLZ/HEP zinc-binding subdomain is critical for regulation of the mitochondrial chaperone HSPA9.Protein science : a publication of the Protein Society · 2012Article
- Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system.Cell stress & chaperones · 2012Article
- The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles.Journal of molecular biology · 2011Article
- Primary sequence that determines the functional overlap between mitochondrial heat shock protein 70 Ssc1 and Ssc3 of Saccharomyces cerevisiae.The Journal of biological chemistry · 2011Article
- Understanding the functional interplay between mammalian mitochondrial Hsp70 chaperone machine components.The Journal of biological chemistry · 2010Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The co-chaperone Hep1 is required to prevent the aggregation of mitochondrial Hsp70 proteins. We have analyzed the interaction of Hep1 with mitochondrial Hsp70 (Ssc1) and the determinants in Ssc1 that make it prone to aggregation. The ATPase and peptide binding domain (PBD) of Hsp70 proteins are connected by a linker segment that mediates interdomain communication between the domains. We show here that the minimal Hep1 binding entity of Ssc1 consists of the ATPase domain and the interdomain linker. In the absence of Hep1, the ATPase domain with the interdomain linker had the tendency to aggregate, in contrast to the ATPase domain with the mutated linker segment or without linker, and in contrast to the PBD. The closest homolog of Ssc1, bacterial DnaK, and a Ssc1 chimera, in which a segment of the ATPase domain of Ssc1 was replaced by the corresponding segment from DnaK, did not aggregate in Delta hep1 mitochondria. The propensity to aggregate appears to be a specific property of the mitochondrial Hsp70 proteins. The ATPase domain in combination with the interdomain linker is crucial for aggregation of Ssc1. In conclusion, our results suggest that interdomain communication makes Ssc1 prone to aggregation. Hep1 counteracts aggregation by binding to this aggregation-prone conformer.
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