Evidence of glutathione transferase complexing and signaling in the model nematode Caenorhabditis elegans using a pull-down proteomic assay

Darren Greetham, Charles Thomas Morgan, Alison Mary Campbell, Arjan Johannes van Rossum, John Barrett, Peter M. Brophy

Research output: Contribution to journalArticlepeer-review

10 Citations (SciVal)

Abstract

Phage display techniques using random peptide interactions have supported the role of mammalian glutathione transferase (GST) as part of a signalling pathway for both oxidative stress and an apoptosis pathway. Little is known about the interaction of nonmammalian GST with other proteins. GSTs have been implicated in the development of chronic nematode infections by neutralising cytotoxic products arising from host immune initiated reactive oxygen species (ROS) assault. In this study we attached one of the key GSTs expressed in the model nematode Caenorhabditis elegans to an affinity support matrix and directly identified major interacting proteins by two-dimensional electrophoresis and peptide mass fingerprinting before and following oxidative stress. Nematode GST does not appear to be a stand-alone enzyme and interacts with many types of proteins in both normal and ROS stress conditions. Pull-down proteomic presents a flexible, label free, rapid and economical assay without specialised ligand fishing equipment to identify protein binding partners.
Original languageEnglish
Pages (from-to)1989-1995
Number of pages7
JournalProteomics
Volume4
Issue number7
Early online date07 Jun 2004
DOIs
Publication statusPublished - Jul 2004

Keywords

  • Caenorhabditis elgans
  • glutathione transferases
  • nematode
  • reactive oxygen species
  • structural genomics

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