Use of the "tag-switch" method for the detection of protein S-sulfhydration.

Chung-Min Park, Igor Macinkovic, Milos R Filipovic, Ming Xian

Journal: Methods in enzymology 2015;555():39-56

PMID: 25747474

Full Text on Elsevier Science View on PubMed

Abstract

Protein S-sulfhydration (i.e., converting protein cysteines -SH to persulfides -SSH) is a redox-based posttranslational modification. This reaction plays an important role in signaling pathways mediated by hydrogen sulfide or other reactive sulfane sulfur species. Recently, our laboratories developed a "tag-switch" method which can be used to selectively label and detect protein S-sulfhydrated residues. In this chapter, we provide a comprehensive summary of this method, including the design of the method, preparation of the reagents, validation on small-molecule substrates, as well as applications in protein labeling. Experimental protocols for the use of the method are described in details.

Address: Department of Chemistry, Washington State University, Pullman, Washington, USA.; Department of Chemistry and Pharmacy, University of Erlangen-Nuremberg, Erlangen, Germany.; Department of Chemistry and Pharmacy, University of Erlangen-Nuremberg, Erlangen, Germany. Electronic address: [email protected].; Department of Chemistry, Washington State University, Pullman, Washington, USA. Electronic address: [email protected].

DOI: 10.1016/bs.mie.2014.11.033

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MeSH Terms: Acetates, Benzothiazoles, Biotin, Cysteine, Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+), Human Umbilical Vein Endothelial Cells, Humans, Hydrogen Sulfide, Jurkat Cells, Microscopy, Fluorescence, Oxidation-Reduction, Protein Processing, Post-Translational, Serum Albumin, Bovine, Signal Transduction, Spectrometry, Mass, Electrospray Ionization, Staining and Labeling, Streptavidin, Sulfides