The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1

Abstract : Glutathione transferases (GSTs) constitute a superfamily of enzymes with essential roles in cellular detoxification and secondary metabolism in plants as in other organisms. Several plant GSTs, including those of the Phi class (GSTFs), require a conserved catalytic serine residue to perform glutathione (GSH)-conjugation reactions. Genomic analyses revealed that terrestrial plants have around ten GSTFs, eight in the Populus trichocarpa genome, but their physiological functions and substrates are mostly unknown. Transcript expression analyses showed a predominant expression of all genes both in reproductive (female flowers, fruits, floral buds) and vegetative organs (leaves, petioles). Here, we show that the recombinant poplar GSTF1 (PttGSTF1) possesses peroxidase activity toward cumene hydroperoxide and GSH-conjugation activity toward model substrates such as 2,4-dinitrochlorobenzene, benzyl and phenetyl isothiocyanate, 4-nitrophenyl butyrate and 4-hydroxy-2-nonenal but interestingly not on previously identified GSTF-class substrates. In accordance with analytical gel filtration data, crystal structure of PttGSTF1 showed a canonical dimeric organization with bound GSH or 2-(N-morpholino)ethanesulfonic acid molecules. The structure of these protein-substrate complexes allowed delineating the residues contributing to both the G and H sites that form the active site cavity. In sum, the presence of GSTF1 transcripts and proteins in most poplar organs especially those rich in secondary metabolites such as flowers and fruits, together with its GSH-conjugation activity and its documented stress-responsive expression suggest that its function is associated with the catalytic transformation of metabolites and/or peroxide removal rather than with ligandin properties as previously reported for other GSTFs.
Type de document :
Article dans une revue
Frontiers in Plant Science, Frontiers, 2014, 5, 〈10.3389/fpls.2014.00712〉
Liste complète des métadonnées

Littérature citée [58 références]  Voir  Masquer  Télécharger

https://hal.univ-lorraine.fr/hal-01521321
Contributeur : Crm2 Ul <>
Soumis le : vendredi 12 mai 2017 - 10:23:33
Dernière modification le : lundi 19 mars 2018 - 12:12:43
Document(s) archivé(s) le : dimanche 13 août 2017 - 12:27:45

Fichier

fpls-05-00712.pdf
Fichiers éditeurs autorisés sur une archive ouverte

Identifiants

Collections

Citation

Henri Pégeot, Cha San Koh, Benjamin Petre, Sandrine Mathiot, Sébastien Duplessis, et al.. The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1. Frontiers in Plant Science, Frontiers, 2014, 5, 〈10.3389/fpls.2014.00712〉. 〈hal-01521321〉

Partager

Métriques

Consultations de la notice

74

Téléchargements de fichiers

54