Oxidized glutathione promotes association between eukaryotic translation elongation factor 1Bγ and Ure2p glutathione transferase from Phanerochaete chrysosporium

The eukaryotic translation elongation factor 1B gamma (eEF1B gamma) is an atypical member of the glutathione transferase (GST) superfamily. Contrary to more classical GSTs having a role in toxic compound detoxification, eEF1B gamma is suggested to act as a scaffold protein, anchoring the elongation factor complex EF1B to the endoplasmic reticulum. In this study, we show that eEF1B gamma from the basidiomycete Phanerochaete chrysosporium is fully active as a glutathione transferase in vitro and undergoes conformational changes upon binding of oxidized glutathione. Using real-time analyses of biomolecular interactions, we show that GSSG allows eEF1B gamma to physically interact with other GSTs from the Ure2p class, opening new perspectives for a better understanding of the role of eEF1B gamma in cellular oxidative stress response.

Automated summary

eEF1B gamma, an atypical member of the GST superfamily, functions as a glutathione transferase in basidiomycete Phanerochaete chrysosporium and undergoes conformational changes upon binding of oxidized glutathione. GSSG enables eEF1B gamma to physically interact with other GSTs from the Ure2p class, offering new insights into its role in cellular oxidative stress response.