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ATP-bound human mtHsp60:mtHsp10 half-football complex (C7), SPA reconstruction

Output Details

Using cryo–electron tomography in human cells, we investigated the structural response of mitochondria to proteostatic stress. Stress induced protein aggregation in the mitochondrial matrix, remodeling of cristae architecture, and a reduction in mitochondrial ribosome complexes, while mitochondrial Hsp60 adopted conformations favoring complexes with its co-chaperone Hsp10 and interacting with native substrates. Complementary high-resolution single-particle cryo-EM reconstructions of mHsp60 provided mechanistic insight into its nucleotide-dependent functional cycle.
Tags
  • Chaperones
  • Cryo-EM
  • Microscopy - electron
  • Mitochondria
  • Proteostasis

Meet the Authors

  • User avatar fallback logo

    Kenneth Ehses

    External Collaborator

  • User avatar fallback logo

    Jorge P. López-Alonso

    External Collaborator

  • User avatar fallback logo

    Odetta Antico

    External Collaborator

  • User avatar fallback logo

    Yannik Lang

    External Collaborator

  • User avatar fallback logo

    Till Rudack

    External Collaborator

  • User avatar fallback logo

    Abdussalam Azem

    External Collaborator

  • Miratul Muqit

    Co-PI (Core Leadership): Team Alessi

    University of Dundee

  • Ruben Fernandez-Busnadiego, PhD

    Co-PI (Core Leadership): Team Harper

    University of Gottingen

Aligning Science Across Parkinson's
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