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14 mai 2018 - Séminaire scientifique "Glutathione transferases in lignocellulose degradation"

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14 mai 2018 - Séminaire scientifique "Glutathione transferases in lignocellulose degradation"

Lieu  : Reims.


Séminaire scientifique intitulé "Glutathione transferases in lignocellulose degradation" présenté par par Mr le Professeur Eric Gelhaye de l’UMR INRA 1136 Interactions Arbres-Microorganismes (IAM) de l’Université de Lorraine, le 14 mai 2018 à 13h30 au sein du CREA (2 Espl. Roland Garros, 51100 Reims).

Wood decaying fungi have developed unique features allowing them to use complex carbon sources. The adaptation of these organisms to their life style is due at least in part of the existence of extracellular degrading systems. Besides these extensively studied extracellular systems of degradation, wood decaying (and more globally complex organic matter degrading) fungi possess also extended detoxification systems in comparison with other fungi belonging to other trophic types. A comparative genomic approach revealed indeed the presence of an extended multigenic family encoding glutathione transferases (GSTs) in the genomes of wood decayers. A phylogenetic analysis revealed that this extension concerns at least four classes of GSTs (omega, FuA, Ure2p and GTT), these extended classes varying in function of the considered fungus. During the last few years, our group has strongly invested in the biochemical and structural characterization of various isoforms from different fungal models and in particular from Phanerochaete chrysosporium. These studies have revealed that the activity of these enzymes could be split off into two functional groups catalyzing opposite reactions, namely : glutathionylation and deglutathionylation. The characterized isoforms are also able to interact with various molecules present in wood from various tree species, such as flavonoids, terpenes or resulting of the wood biodegradation. Some of these fungal GSTs are also structurally related to the bacterial GSTs involved in lignin degradation. In these bacterial systems, some GSTs exhibit an activity of β-O-4 ether cleavage through a glutathionylation activity, whereas other isoforms are involved in the recycling of glutathione through an activity of deglutathionylation. From these structural and biochemical studies, we will discuss the physiological functions of this multigenic family of GSTs in relation with the degradation of complex biomass and their potential use in biotechnology.

Inscriptions auprès de :
Harivony Rakotoarivonina : harivony.rakotoarivonina@univ-reims.fr
Gabriel Paës : gabriel.paes@inra.fr

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