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MitCHAP-60 and Hereditary Spastic Paraplegia SPG-13 Arise from an Inactive hsp60 Chaperonin that Fails to Fold the ATP Synthase β-Subunit

Sci Rep.. 2019; 
Wang J1, Enriquez AS1, Li J1, Rodriguez A1, Holguin B1, Von Salzen D1, Bhatt JM2, Bernal RA3.
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Molecular Biology Reagents … Paso. pET-26b vectors encoding the human ATP synthase F 1 α-subunit (ATP5F1A)<br> and human ATP synthase F 1 β-subunit (ATP5F1B) were purchased from <b>GenScript</b>.<br> Protein expression and purification. Unless otherwise … Get A Quote

摘要

The human mitochondrial heat shock protein 60 (hsp60) is a tetradecameric chaperonin that folds proteins in the mitochondrial matrix. An hsp60 D3G mutation leads to MitCHAP-60, an early onset neurodegenerative disease while hsp60 V72I has been linked to SPG13, a form of hereditary spastic paraplegia. Previous studies have suggested that these mutations impair the protein folding activity of hsp60 complexes but the detailed mechanism by which these mutations lead the neuromuscular diseases remains unknown. It is known, is that the β-subunit of the human mitochondrial ATP synthase co-immunoprecipitates with hsp60 indicating that the β-subunit is likely a substrate for the chaperonin. Therefore, we hypothesized ... More

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