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Microfluidic Mixers for Studying Protein Folding
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Disulfide driven folding for a conditionally disordered protein.

Hugo Fraga1,2,3, Jordi Pujols1,2, Marcos Gil-Garcia1,2

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Conditionally disordered proteins, like human Cox17, switch between unfolded and folded states. This study reveals a single disulfide bond controls this transition, enabling mitochondrial protein import and function.

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Area of Science:

  • Mitochondrial protein import and biogenesis
  • Protein folding and conformational dynamics
  • Molecular mechanisms of conditionally disordered proteins

Background:

  • Mitochondrial intermembrane space (IMS) proteins, such as Mia40 substrates, are synthesized in the cytosol and must fold in the IMS.
  • These proteins exhibit conditional disorder, existing as unfolded or folded states based on environmental cues.
  • The molecular basis for sequences encoding both unfolded and folded states remains unclear.

Purpose of the Study:

  • To investigate the disorder-to-order transition mechanism of the human small copper chaperone Cox17, a Mia40 substrate.
  • To elucidate how a single protein sequence can mediate both protein translocation and functional folding.
  • To provide molecular insights into the regulation of protein folding in the mitochondrial IMS.

Main Methods:

  • Integrated real-time analysis using chromatography, fluorescence, circular dichroism (CD), Fourier-transform infrared spectroscopy (FTIR), small-angle X-ray scattering (SAXS), nuclear magnetic resonance (NMR), and mass spectrometry (MS).
  • Characterization of Cox17 conformational changes under various conditions.
  • Assessment of the role of disulfide bond formation in the folding process.

Main Results:

  • Demonstrated that the conformational switch of Cox17 between disordered and folded states is regulated by the formation of a single disulfide bond.
  • Showed this disulfide bond-mediated transition occurs irrespective of the presence or absence of Mia40.
  • Provided molecular details on the tightly regulated, spatiotemporal folding of a conditionally disordered protein.

Conclusions:

  • The formation of a single disulfide bond is the key determinant for the disorder-to-order transition in the human Cox17 protein.
  • This mechanism ensures that the same protein sequence is competent for both translocation into the mitochondria and subsequent functional activity.
  • Highlights a precise regulatory mechanism for protein folding within the mitochondrial intermembrane space.