par Pócsi, István;Prade, Rolf A;Penninckx, Michel
Référence Advances in Microbial Physiology, 49, page (1-76)
Publication Publié, 2004
Article révisé par les pairs
Résumé : Glutathione (GSH; gamma-L-glutamyl-L-cysteinyl-glycine), a non-protein thiol with a very low redox potential (E'0 = 240 mV for thiol-disulfide exchange), is present in high concentration up to 10 mM in yeasts and filamentous fungi. GSH is concerned with basic cellular functions as well as the maintenance of mitochondrial structure, membrane integrity, and in cell differentiation and development. GSH plays key roles in the response to several stress situations in fungi. For example, GSH is an important antioxidant molecule, which reacts non-enzymatically with a series of reactive oxygen species. In addition, the response to oxidative stress also involves GSH biosynthesis enzymes, NADPH-dependent GSH-regenerating reductase, glutathione S-transferase along with peroxide-eliminating glutathione peroxidase and glutaredoxins. Some components of the GSH-dependent antioxidative defence system confer resistance against heat shock and osmotic stress. Formation of protein-SSG mixed disulfides results in protection against desiccation-induced oxidative injuries in lichens. Intracellular GSH and GSH-derived phytochelatins hinder the progression of heavy metal-initiated cell injuries by chelating and sequestering the metal ions themselves and/or by eliminating reactive oxygen species. In fungi, GSH is mobilized to ensure cellular maintenance under sulfur or nitrogen starvation. Moreover, adaptation to carbon deprivation stress results in an increased tolerance to oxidative stress, which involves the induction of GSH-dependent elements of the antioxidant defence system. GSH-dependent detoxification processes concern the elimination of toxic endogenous metabolites, such as excess formaldehyde produced during the growth of the methylotrophic yeasts, by formaldehyde dehydrogenase and methylglyoxal, a by-product of glycolysis, by the glyoxalase pathway. Detoxification of xenobiotics, such as halogenated aromatic and alkylating agents, relies on glutathione S-transferases. In yeast, these enzymes may participate in the elimination of toxic intermediates that accumulate in stationary phase and/or act in a similar fashion as heat shock proteins. GSH S-conjugates may also form in a glutathione S-transferases-independent way, e.g. through chemical reaction between GSH and the antifugal agent Thiram. GSH-dependent detoxification of penicillin side-chain precursors was shown in Penicillium sp. GSH controls aging and autolysis in several fungal species, and possesses an anti-apoptotic feature.