Identification of NoxD/Pro41 as the homologue of the p22^phoxNADPH oxidase subunit in fungi

Chasing stress signals – Exposure to extracellular stimuli differentially affects the redox state of cell compartments in the wild type and signaling mutants of Botrytis cinerea

“…Although many aspects of their function in fungi are still unknown, there is increasing evidence of structural/functional homologies between Nox complexes in mammals and fungi, despite of the evolutionary distance. For example, homologs of the regulatory subunit (p67phox/NoxR), the catalytic subunit (gp91phox/Nox1/2 or NoxA/B) as well as other regulatory compounds (p22phox/ NoxD) (Cano-Dominguez et al, 2008;Egan et al, 2007;Lacaze et al, 2015;Lara-Ortiz et al, 2003;Malagnac et al, 2004;Segmueller et al, 2008;Semighini and Harris, 2008;Siegmund et al, 2013Siegmund et al, , 2015 have been already identified and characterized. To handle elevated levels of ROS, eukaryotic cells have evolved scavenging systems to establish and maintain an equilibrium.…”

Reactive oxygen species metabolism and plant-fungal interactions

“…Fungi possess three Nox enzymes; NoxA (also known as Nox1) and NoxB (also known as Nox2) are homologous of the gp91 phox catalytic subunit while NoxC carries a Ca 2+ -binding EF hand and is similar to mammalian Nox5 (Aguirre et al, 2005;Heller and Tudzynski, 2011;Ryder et al, 2013). Nox requires adapter proteins for function, yet the homolog of the adaptor protein p22 phox (NoxD) has only recently been characterized in Podospora anserina, Botrytis cinerea and Magnaporthe oryzae (Lacaze et al, 2015;Scott, 2015;Siegmund et al, 2015;Galhano et al, 2017). NoxD acts with Nox1 in P. anserina and NoxA in B. cinerea, and NoxD deletion strains in these fungi are phenotypically identical to the respective Nox1/NoxA mutant, suggesting they act together (Lacaze et al, 2015;Scott, 2015;Siegmund et al, 2015).…”

“…Nox requires adapter proteins for function, yet the homolog of the adaptor protein p22 phox (NoxD) has only recently been characterized in Podospora anserina, Botrytis cinerea and Magnaporthe oryzae (Lacaze et al, 2015;Scott, 2015;Siegmund et al, 2015;Galhano et al, 2017). NoxD acts with Nox1 in P. anserina and NoxA in B. cinerea, and NoxD deletion strains in these fungi are phenotypically identical to the respective Nox1/NoxA mutant, suggesting they act together (Lacaze et al, 2015;Scott, 2015;Siegmund et al, 2015). In M. oryzae, Nox1 and NoxD interact-but participate differently in septinmediated cytoskeleton organization-indicating the fungal NADPH oxidase complex is dynamic (Galhano et al, 2017).…”

Plant biomass degrading ability of the coprophilic ascomycete fungus Podospora anserina

“…Genetic analysis has shown that the production of the P. anserina appressorium-like structures is under the control of signalling pathways, which include the PaMpk2/PaMKK2/PaTLK2 MAP kinase module, as well as the PaNox1 and PaNox2 NADPH oxidase enzymes and their regulatory subunits, PaNoxD/PaNoxR and PaPls1/PaNoxR, respectively (Brun et al, 2009;Lalucque et al, 2012;Lacaze et al, 2015). However, it does not depend on the PaMpk1 or PaMpk3 pathways or the PaNox3 NADPH oxidase (Brun et al, 2009;Lalucque et al, 2012).…”