title: Glutathione-S-transferase-fusion based assays for studying protein-protein interactions.
abstract: Glutathione-S-transferase (GST)-fusion proteins have become an effective reagent to use in the study of protein-protein interactions. They can be produced in bacterial and mammalian cells in large quantities and purified rapidly. Given that GST can be coupled to a glutathione matrix permits its use as an effective affinity column to study interactions in vitro or to purify protein complexes in cells expressing the GST-fusion. Here we provide a technical description on the utilization of GST-fusion proteins as both a tool to studying protein-protein interactions and also as a means to purify interacting proteins.
authors.affiliation: Department of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA.
authors.forename: Haris G
authors.initials: HG
authors.lastname: Vikis
authors.forename: Kun-Liang
authors.initials: KL
authors.lastname: Guan
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase