Chapter 6 Reactive Oxygen Species in Phanerochaete chrysosporium Relationship Between Extracellular Oxidative and Intracellular Antioxidant Systems

Morel, Mélanie; Ngadin, Andrew A.; Jacquot, Jean‐Pierre; Gelhaye, Éric

doi:10.1016/s0065-2296(10)52006-8

Cited by 11 publications

(8 citation statements)

References 122 publications

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“…Additionally, the DPaMpk2 mutants had an abnormal pattern of staining with DAB and NBT, which are supposed to measure accumulation of peroxides and superoxides, respectively ( Figure S3) (Munkres 1990). This shows that mycelium redox activities are modified in the DPaMpk2 mutants as in the DPaMpk1 mutants (Malagnac et al 2004) and is in line with their impaired ability to degrade cellulose as redox activities are known to be involved in the degradation of this polysaccharide (Morel et al 2009). Unlike the DPaMpk1 mutants, the DPaMpk2 mutants were slightly affected in hyphal interference, a defense mechanism exerted by P. anserina when it encounters another filamentous fungus (Silar 2005).…”

Section: Mycelium Growth and Differentiation In The Mapk Mutantsmentioning

confidence: 63%

A Non-Mendelian MAPK-Generated Hereditary Unit Controlled by a Second MAPK Pathway inPodospora anserina

et al. 2012

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The Podospora anserina PaMpk1 MAP kinase (MAPK) signaling pathway can generate a cytoplasmic and infectious element resembling prions. When present in the cells, this C element causes the crippled growth (CG) cell degeneration. CG results from the inappropriate autocatalytic activation of the PaMpk1 MAPK pathway during growth, whereas this cascade normally signals stationary phase. Little is known about the control of such prion-like hereditary units involved in regulatory inheritance. Here, we show that another MAPK pathway, PaMpk2, is crucial at every stage of the fungus life cycle, in particular those controlled by PaMpk1 during stationary phase, which includes the generation of C. Inactivation of the third P. anserina MAPK pathway, PaMpk3, has no effect on the development of the fungus. Mutants of MAPK, MAPK kinase, and MAPK kinase kinase of the PaMpk2 pathway are unable to present CG. This inability likely relies upon an incorrect activation of PaMpk1, although this MAPK is normally phosphorylated in the mutants. In PaMpk2 null mutants, hyphae are abnormal and PaMpk1 is mislocalized. Correspondingly, stationary phase differentiations controlled by PaMpk1 are defective in the mutants of the PaMpk2 cascade. Constitutive activation of the PaMpk2 pathway mimics in many ways its inactivation, including an effect on PaMpk1 localization. Analysis of double and triple mutants inactivated for two or all three MAPK genes undercover new growth and differentiation phenotypes, suggesting overlapping roles. Our data underscore the complex regulation of a prion-like element in a model organism.

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Section: Mycelium Growth and Differentiation In The Mapk Mutantsmentioning

confidence: 63%

A Non-Mendelian MAPK-Generated Hereditary Unit Controlled by a Second MAPK Pathway inPodospora anserina

et al. 2012

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“…Phanerochaete chrysosporium is considered as the model organism to study the physiology of white rot fungi, the only known microorganisms able to completely break down lignin to carbon dioxide and water (1)(2)(3). Analysis of the genome of this basidiomycete revealed a complex superfamily of cytochrome P450 monooxygenases representing around 1% of this genome (1,4).…”

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confidence: 99%

“…Based on primary structure similarity, these cytosolic GSTs belong to seven different classes as follows: Ure2p-like, GTT1, GTT2, EFB␥, MAK16, etherases, and Omega (GSTO) 3 (9). Among the cytosolic GSTs, P. chrysosporium exhibits eight putative proteins showing homology with GSTs of the Omega class, named PcGSTO1 to PcGSTO8.…”

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confidence: 99%

Glutathione Transferases of Phanerochaete chrysosporium

Meux

Prosper²,

Ngadin

et al. 2011

Journal of Biological Chemistry

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The white rot fungus Phanerochaete chrysosporium, a saprophytic basidiomycete, possesses a large number of cytosolic glutathione transferases, eight of them showing similarity to the Omega class. PcGSTO1 (subclass I, the bacterial homologs of which were recently proposed, based on their enzymatic function, to constitute a new class of glutathione transferase named S-glutathionyl-(chloro)hydroquinone reductases) and PcGSTO3 (subclass II related to mammalian homologs) have been investigated in this study. Biochemical investigations demonstrate that both enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteinyl residue. This reaction leads to the formation of a disulfide bridge between the conserved cysteine and the removed glutathione from their substrate. The substrate specificity of each isoform differs. In particular PcGSTO1, in contrast to PcGSTO3, was found to catalyze deglutathionylation of S-glutathionyl-p-hydroquinone substrates. The three-dimensional structure of PcGSTO1 presented here confirms the hypothesis that it belongs not only to a new biological class but also to a new structural class that we propose to name GST xi. Indeed, it shows specific features, the most striking ones being a new dimerization mode and a catalytic site that is buried due to the presence of long loops and that contains the catalytic cysteine.

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“…First, they participate in the degradation of the plant biomass, especially lignin lysis (ten Have & Teunissen 2001;Wesenberg et al 2003;Martinez et al 2005;Morel et al 2009). Second, they are involved in signaling several developmental processes, including fruiting body maturation (Lara-Ortiz et al 2003;Malagnac et al 2004), spore germination (Malagnac et al 2004;Cano-Dominguez et al 2008;Lambou et al 2008), mycelium growth (Leuthner et al 2005;Semighini & Harris 2008), mutualistic symbiosis (Tanaka et al 2006) and differentiation of appressorium and appressorium-like structures (Egan et al 2007;Segmuller et al 2008;Brun et al 2009).…”

Section: Introductionmentioning

confidence: 99%

“…In these species several ROS producing enzymes have been implicated in plant biomass degradation, including laccases, GMC oxidoreductases, galactose oxidases, copper radical oxidases (e.g. glyoxal oxidase), quinone reductases, pyranose oxidases and cellobiose dehydrogenases (ten Have & Teunissen 2001; Wesenberg et al 2003;Martinez et al 2005;Morel et al 2009). From one fungus to the other the enzymology of plant biomass degradation appears different.…”

Section: Introductionmentioning

confidence: 99%