Ladomery Lab RNA Biology Group


Ladomery Lab
Southwest UK RNA Club

Invited Reviews

Detection of thiol modifications by hydrogen sulphide

Methods in Enzymology 555, 233-251 (2015) -

Authors: Williams E, Pead S, Whiteman M, Wood ME, Wilson ID, Ladomery MR, Teklic Tl, Lisjak M, Hancock JT

Abstract

Hydrogen sulfide (H2S) is an important gasotransmitter in both animals and plants. Many physiological events, including responses to stress, have been suggested to involved H2S, at least in part. On the other hand, numerous responses have been reported following treatment with H2S, including changes in the levels of antioxidants and the activities of transcription factors. Therefore, it is important to understand and unravel the events that are taking place downstream of H2S in signalling pathways. H2S is known to interact with other reactive singalling molecules such as reactive oxygen species (ROS) and nitric oxide (NO). One of the mechanisms by which ROS and NO have effects in a cell is the modification of thiol groups on proteins, by oxidation or S-nitrosylation, respectively. Recently, it has been reported that H2S can also modify thiols. Here we report a method for the determination of thiol modifications on proteins following the treatment with biological samples with H2S donors. Here, the nematode Caenorhabditis elegans is used as a model system but this method can be used for samples from other animals or plants.

Keywords: Hydrogen sulfide,gasotransmitters,cell signalling,modified thiols,Caenorhabditis elegans