ArticleCell cycle (Georgetown, Tex.)2017
The human mitochondrial Hsp60 in the APO conformation forms a stable tetradecameric complex.
Article in Cell cycle (Georgetown, Tex.), 2017. 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.
- Cryo-EM of a heterogeneous biochemical fraction elucidates multiple protein complexes from a multicellular thermophilic eukaryote.Journal of structural biology: X · 2023Article
- Hereditary spastic paraplegia SPG13 mutation increases structural stability and ATPase activity of human mitochondrial chaperonin.Scientific reports · 2022Article
- Insights Into the Role of Heat Shock Protein 27 in the Development of Neurodegeneration.Frontiers in molecular neuroscience · 2022Review
- Host cell stress response as a predictor of COVID-19 infectivity and disease progression.Frontiers in molecular biosciences · 2022Review
- Heat shock proteins with an emphasis on HSP 60.Molecular biology reports · 2021Review
- Structural basis for the structural dynamics of human mitochondrial chaperonin mHsp60.Scientific reports · 2021Article
- Complex Destabilization in the Mitochondrial Chaperonin Hsp60 Leads to Disease.Frontiers in molecular biosciences · 2020Review
- Hsp60 Post-translational Modifications: Functional and Pathological Consequences.Frontiers in molecular biosciences · 2020Review
- Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of α-Synuclein.International journal of molecular sciences · 2019Article
- MitCHAP-60 and Hereditary Spastic Paraplegia SPG-13 Arise from an Inactive hsp60 Chaperonin that Fails to Fold the ATP Synthase β-Subunit.Scientific reports · 2019Article
- Regulation of stress signaling pathways by protein lipoxidation.Redox biology · 2019Review
- Single-Ring Intermediates Are Essential for Some Chaperonins.Frontiers in molecular biosciences · 2018Article
- Chaperonin of Group I: Oligomeric Spectrum and Biochemical and Biological Implications.Frontiers in molecular biosciences · 2017Review
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Authors and funding
6 authors.
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Abstract
The human mitochondrial chaperonin is a macromolecular machine that catalyzes the proper folding of mitochondrial proteins and is of vital importance to all cells. This chaperonin is composed of 2 distinct proteins, Hsp60 and Hsp10, that assemble into large oligomeric complexes that mediate the folding of non-native polypeptides in an ATP dependent manner. Here, we report the bacterial expression and purification of fully assembled human Hsp60 and Hsp10 recombinant proteins and that Hsp60 forms a stable tetradecameric double-ring conformation in the absence of co-chaperonin and nucleotide. Evidence of the stable double-ring conformation is illustrated by the 15 Å resolution electron microscopy reconstruction presented here. Furthermore, our biochemical analyses reveal that the presence of a non-native substrate initiates ATP-hydrolysis within the Hsp60/10 chaperonin to commence protein folding. Collectively, these data provide insight into the architecture of the intermediates used by the human mitochondrial chaperonin along its protein folding pathway and lay a foundation for subsequent high resolution structural investigations into the conformational changes of the mitochondrial chaperonin.
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