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In situ observation of chaperonin function in protein folding

ABSTRACT: The GroEL/GroES chaperonin mediates protein folding in bacteria in an ATP-dependent process. Studies in vitro show that the GroEL double-ring and the lid-shaped GroES transiently encapsulate unfolded protein for folding unimpaired by aggregation. To clarify critical aspects of this mechanism, we used cryo-electron tomography in situ to visualize and quantify functional GroEL:ES complexes in their intact cellular environment. Mass spectrometry was used to estimate stoichiometries of GroEL, GroES, cellular ribosome content and substrates.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Escherichia Coli

SUBMITTER: Roman Körner

LAB HEAD: F. Ulrich Hartl

PROVIDER: PXD042587 | Pride | 2024-06-27

REPOSITORIES: Pride

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Project description:Please provide an overall description of your study, think something similar in scope to the manuscript abstractCell proteostasiCell proteostasis includes gene transcription, protein translation, folding of de novo proteins, post-translational modification, secretion, degradation and recycling. By profiling the proteome of extracellular vesicles (EVs) from T cells, we have found the chaperonin complex CCT, involved in the correct folding of particular proteins. By limiting CCT cell-content by siRNA, cells undergo altered lipid composition and metabolic rewiring towards a lipid-dependent metabolism, with increased activity of peroxisomes and mitochondria. This is due to dysregulation of the dynamics of interorganellar contacts between lipid droplets, mitochondria, peroxisomes and the endolysosomal system. This process accelerates the biogenesis of multivesicular bodies leading to higher EV production through the dynamic regulation of microtubule-based kinesin motors. These findings connect proteostasis with lipid metabolism through an unexpected role of CCT.s includes gene transcription, protein translation, folding of de novo proteins, post-translational modification, secretion, degradation and recycling. By profiling the proteome of extracellular vesicles (EVs) from T cells, we have found the chaperonin complex CCT, involved in the correct folding of particular proteins. By limiting CCT cell-content by siRNA, cells undergo altered lipid composition and metabolic rewiring towards a lipid-dependent metabolism, with increased activity of peroxisomes and mitochondria. This is due to dysregulation of the dynamics of interorganellar contacts between lipid droplets, mitochondria, peroxisomes and the endolysosomal system. This process accelerates the biogenesis of multivesicular bodies leading to higher EV production through the dynamic regulation of microtubule-based kinesin motors. These findings connect proteostasis with lipid metabolism through an unexpected role of CCT.

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In situ observation of chaperonin function in protein folding

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