A crosslinker-based identification of redox relay targets

Anal Biochem. 2017 Mar 1:520:22-26. doi: 10.1016/j.ab.2016.12.025. Epub 2016 Dec 31.

Abstract

Thiol-based redox control is among the most important mechanisms for maintaining cellular redox homeostasis, with essential participation of cysteine thiols of oxidoreductases. To explore cellular redox regulatory networks, direct interactions among active cysteine thiols of oxidoreductases and their targets must be clarified. We applied a recently described thiol-ene crosslinking-based strategy, named divinyl sulfone (DVSF) method, enabling identification of new potential redox relay partners of the cytosolic oxidoreductases thioredoxin (TXN) and thioredoxin domain containing 17 (TXNDC17). Applying multiple methods, including classical substrate-trapping techniques, will increase understanding of redox regulatory mechanisms in cells.

Keywords: Interaction; Oxidoreductase; Proteomics; Redox; Thioredoxin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cross-Linking Reagents / chemistry*
  • HEK293 Cells
  • Humans
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Sequence Alignment
  • Sulfones / chemistry
  • Thioredoxins / chemistry
  • Thioredoxins / genetics
  • Thioredoxins / metabolism*

Substances

  • Cross-Linking Reagents
  • Sulfones
  • TXNDC17 protein, human
  • Thioredoxins
  • divinyl sulfone