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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates.

Catherine S Chan1, Limei Chang, Tara M L Winstone

  • 1Department of Biological Sciences, Faculty of Science, University of Calgary, Calgary, Alberta, Canada.

FEBS Letters
|October 27, 2010
PubMed
Summary

Redox enzyme maturation proteins (REMPs) bind twin-arginine translocation (Tat) substrates. Interactions occur with the preprotein, regardless of leader cleavage, and can involve specific regions like the leader peptide or mature protein.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • The twin-arginine translocation (Tat) system transports folded proteins across membranes.
  • Redox enzymes utilizing the Tat system require specific chaperones, known as redox enzyme maturation proteins (REMPs), for proper folding and maturation.
  • Tat substrates are characterized by an RR-motif in their leader peptide.

Purpose of the Study:

  • To investigate the specific regions of Tat substrate preproteins that interact with their cognate REMPs.
  • To determine if the leader peptide or mature protein domains are critical for REMP binding.
  • To assess the impact of the leader cleavage site on chaperone-substrate interactions.

Main Methods:

  • Assaying interactions between various regions of RR-containing oxidoreductase subunits (leader peptide, full preprotein with/without leader cleavage site, mature protein) and their REMPs.
  • Utilizing binding assays to detect chaperone-substrate complex formation.
  • Observing the effects of Tat system absence on chaperone-substrate interaction dynamics.

Main Results:

  • All tested REMPs successfully bound their preprotein substrates, irrespective of the leader cleavage site.
  • Specific REMPs exhibited binding preferences for either the leader peptide or the mature protein region of the substrate.
  • In one instance, REMP binding was exclusively observed with the full preprotein, not isolated domains.
  • The absence of the Tat system affected the overall quantity of chaperone-substrate interactions.

Conclusions:

  • REMP binding to Tat substrates is a robust process, not dependent on leader peptide cleavage.
  • Both the leader peptide and mature protein can mediate REMP interactions, with some REMPs showing domain specificity.
  • The Tat system itself plays a role in modulating the extent of chaperone-substrate engagement.
  • These findings elucidate the molecular basis of redox enzyme maturation within the Tat pathway.