Table of Contents
International Journal of Evolutionary Biology
Volume 2011 (2011), Article ID 938308, 9 pages
Research Article

Functional Diversification of Fungal Glutathione Transferases from the Ure2p Class

1Unité Mixte de Recherches INRA UHP 1136 Interaction Arbres Microorganismes, IFR 110 Ecosystèmes Forestiers, Agroressources, Bioprocédés et Alimentation, Faculté des Sciences et Technologies, Nancy Université BP 70239, 54506 Vandoeuvre-lès-Nancy Cedex, France
2Department of Biological Sciences, Faculty of Science and Technology, Universiti Malaysia Terengganu, 21030 Kuala Terengganu, Malaysia
3Laboratoire des Interactions Microorganismes-Minéraux-Matière Organique dans les Sols, UMR 7137 CNRS—UHP, Faculté des Sciences et Technologies, Nancy Université BP 70239, 54506 Vandoeuvre-lès-Nancy Cedex, France

Received 30 June 2011; Revised 12 August 2011; Accepted 5 September 2011

Academic Editor: Olga C. Nunes

Copyright © 2011 Anne Thuillier et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The glutathione-S-transferase (GST) proteins represent an extended family involved in detoxification processes. They are divided into various classes with high diversity in various organisms. The Ure2p class is especially expanded in saprophytic fungi compared to other fungi. This class is subdivided into two subclasses named Ure2pA and Ure2pB, which have rapidly diversified among fungal phyla. We have focused our analysis on Basidiomycetes and used Phanerochaete chrysosporium as a model to correlate the sequence diversity with the functional diversity of these glutathione transferases. The results show that among the nine isoforms found in P. chrysosporium, two belonging to Ure2pA subclass are exclusively expressed at the transcriptional level in presence of polycyclic aromatic compounds. Moreover, we have highlighted differential catalytic activities and substrate specificities between Ure2pA and Ure2pB isoforms. This diversity of sequence and function suggests that fungal Ure2p sequences have evolved rapidly in response to environmental constraints.