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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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The multidomain thioredoxin-monothiol glutaredoxins represent a distinct functional group.

Bastian Hoffmann1, Marta A Uzarska, Carsten Berndt

  • 1Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Germany.

Antioxidants & Redox Signaling
|February 9, 2011
PubMed
Summary

Multidomain glutaredoxins (Grxs) are essential for iron trafficking in yeast, requiring a specific active site and thioredoxin domain. These proteins form a distinct family from single-domain Grxs, acting as iron sensors for transcription factors.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Yeast Genetics

Background:

  • Monothiol glutaredoxins (Grxs) with CGFS active sites are widespread.
  • Multidomain Grxs, like Grx3 and Grx4 in Saccharomyces cerevisiae, are vital for intracellular iron trafficking.
  • Iron-sulfur (Fe/S) cofactors are crucial for the function of these multidomain Grxs.

Purpose of the Study:

  • To investigate the functional differences between single-domain and multidomain monothiol Grxs.
  • To determine the role of the thioredoxin domain and active site motif in Fe/S cofactor binding and function.
  • To elucidate the mechanism by which Grx4 acts as an iron sensor for the transcription factor Aft1.

Main Methods:

  • Comparative analysis of single-domain and multidomain Grxs.
  • Site-directed mutagenesis to analyze active site motifs (CPxS vs. dithiol).
  • In vivo functional assays and protein-protein interaction studies (Aft1-Grx4 binding).

Main Results:

  • The thioredoxin domain is indispensable for the in vivo function of multidomain Grxs in iron trafficking.
  • A CPxS active site motif supports Fe/S cluster binding on Grx4, while a dithiol active site destabilizes the cofactor.
  • Grx4 directly binds Aft1 at its C-terminus, regulating the transcription factor's activity.
  • Multidomain monothiol Grxs represent a distinct protein family compared to single-domain Grxs.

Conclusions:

  • Multidomain monothiol Grxs possess unique requirements for Fe/S cofactor stabilization, distinct from single-domain Grxs.
  • The thioredoxin domain and specific active site are critical for the iron trafficking role of Grx4.
  • Grx4 functions as an iron sensor through direct interaction with the transcription factor Aft1, highlighting a specialized role for multidomain Grxs.