Detection of protein S-sulfhydration by a tag-switch technique

Angew Chem Int Ed Engl. 2014 Jan 7;53(2):575-81. doi: 10.1002/anie.201305876. Epub 2013 Nov 29.

Abstract

Protein S-sulfhydration (forming -S-SH adducts from cysteine residues) is a newly defined oxidative posttranslational modification and plays an important role in H2 S-mediated signaling pathways. In this study we report the first selective, "tag-switch" method which can directly label protein S-sulfhydrated residues by forming stable thioether conjugates. Furthermore we demonstrate that H2 S alone cannot lead to S-sulfhydration and that the two possible physiological mechanisms include reaction with protein sulfenic acids (P-SOH) or the involvement of metal centers which would facilitate the oxidation of H2 S to HS(.) .

Keywords: hydrogen sulfide; protein S-sulfhydration; signal transduction; tag-switch; thiols.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biotin / chemistry
  • Cysteine / chemistry*
  • Glutathione Peroxidase / chemistry
  • Human Umbilical Vein Endothelial Cells
  • Humans
  • Hydrogen Sulfide / chemistry*
  • Jurkat Cells
  • Microscopy, Fluorescence
  • Protein Processing, Post-Translational*
  • Serum Albumin, Bovine / chemistry
  • Sulfhydryl Compounds / chemistry*
  • Sulfides / chemistry*

Substances

  • Sulfhydryl Compounds
  • Sulfides
  • persulfides
  • Serum Albumin, Bovine
  • Biotin
  • GPX3 protein, human
  • Glutathione Peroxidase
  • Cysteine
  • Hydrogen Sulfide