Two NADPH oxidase isoforms are required for sexual reproduction and ascospore germination in the filamentous fungus Podospora anserina

Malagnac, Fabienne; Lalucque, Hervé; Lepère, Gersende; Silar, Philippe

doi:10.1016/j.fgb.2004.07.008

Cited by 224 publications

(341 citation statements)

References 40 publications

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“…Similarly, previous work in other fungi indicates that nox1 orthologues play rather specific roles in fungal development, as observed in N. crassa, where ROS are generated at the start of each of the morphogenetic steps that occur during asexual development (Hansberg et al, 1993), and correlate with the oxidation of proteins (Toledo et al, 1994). Similar blockages in fruiting body development have been observed in Podospora anserina and N. crassa after nox1 deletion, demonstrating that Nox enzymes are critical for the development of sexual structures in filamentous fungi (Aguirre et al, 2005;Malagnac et al, 2004). Disruption of noxA in A. nidulans blocks sexual development, since differentiation of fruiting bodies cannot be completed (Lara-Ortíz et al, 2003).…”

Section: Ros Drive the Conidiation Processsupporting

confidence: 57%

“…In zebrafish, it has been shown that light induces the production of H 2 O 2 (Hirayama et al, 2007), and in T. atroviride, there is production of ROS upon mechanical injury (M. Hernández-Oñate and others, unpublished results). NADPH oxidases (Nox) have been characterized as enzymes of higher eukaryotes responsible for the production of ROS (Malagnac et al, 2004). The best-studied mammalian gp91 phox (Nox2) requires for its activity the assembly of a multi-subunit complex formed by the cytosolic regulatory component Rac, p40 phox , p47 phox , p67 phox and the integral membrane protein flavocytochrome b 558 , composed of the catalytic subunit gp91 phox and the adaptor protein p22 phox (Scott & Eaton, 2008).…”

Section: Ros Drive the Conidiation Processmentioning

confidence: 99%

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Trichoderma: sensing the environment for survival and dispersal

2012

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Section: Ros Drive the Conidiation Processsupporting

confidence: 57%

Section: Ros Drive the Conidiation Processmentioning

confidence: 99%

Trichoderma: sensing the environment for survival and dispersal

2012

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“…Here, the localization of Mn oxides at the base of reproductive structures implicates processes associated with cell differentiation in Mn(II) oxidation. In particular, superoxide, a known oxidant of Mn(II) (16), is believed to act as both an intracellular and extracellular cell signal for the initiation of asexual and sexual reproductive structures in fungi (28).…”

Section: Resultsmentioning

confidence: 99%

Mn(II) oxidation by an ascomycete fungus is linked to superoxide production during asexual reproduction

Hansel

Zeiner

Santelli

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

199

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Manganese (Mn) oxides are among the most reactive minerals within the environment, where they control the bioavailability of carbon, nutrients, and numerous metals. Although the ability of microorganisms to oxidize Mn(II) to Mn(III/IV) oxides is scattered throughout the bacterial and fungal domains of life, the mechanism and physiological basis for Mn(II) oxidation remains an enigma. Here, we use a combination of compound-specific chemical assays, microspectroscopy, and electron microscopy to show that a common Ascomycete filamentous fungus, Stilbella aciculosa , oxidizes Mn(II) to Mn oxides by producing extracellular superoxide during cell differentiation. The reactive Mn oxide phase birnessite and the reactive oxygen species superoxide and hydrogen peroxide are colocalized at the base of asexual reproductive structures. Mn oxide formation is not observed in the presence of superoxide scavengers (e.g., Cu) and inhibitors of NADPH oxidases (e.g., diphenylene iodonium chloride), enzymes responsible for superoxide production and cell differentiation in fungi. Considering the recent identification of Mn(II) oxidation by NADH oxidase-based superoxide production by a common marine bacterium ( Roseobacter sp.), these results introduce a surprising homology between some prokaryotic and eukaryotic organisms in the mechanisms responsible for Mn(II) oxidation, where oxidation appears to be a side reaction of extracellular superoxide production. Given the versatility of superoxide as a redox reactant and the widespread ability of fungi to produce superoxide, this microbial extracellular superoxide production may play a central role in the cycling and bioavailability of metals (e.g., Hg, Fe, Mn) and carbon in natural systems.

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“…The filamentous fungi Podospora anserina, Neurospora crassa (12) and the social amoeba Dictostelium discoideum (13) could be shown to express NADPH oxidases that actively produce superoxide (14). The deletion of PaNOX1 has no influence on growth, but completely blocks fruiting body formation (14). Fungal NOX enzymes mostly produce ROS as second messengers for coordination of multicellular communication To whom correspondence may be addressed.…”

mentioning

confidence: 99%

“…1073/pnas.1201629109/-/DCSupplemental. (14). However, in hemiascomycetous yeasts no gene or enzyme has been assigned as a superoxide-generating NADPH oxidase up to now (10,15).…”

mentioning

confidence: 99%

Yno1p/Aim14p, a NADPH-oxidase ortholog, controls extramitochondrial reactive oxygen species generation, apoptosis, and actin cable formation in yeast

Rinnerthaler

Büttner

Laun

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

132

136

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The large protein superfamily of NADPH oxidases (NOX enzymes) is found in members of all eukaryotic kingdoms: animals, plants, fungi, and protists. The physiological functions of these NOX enzymes range from defense to specialized oxidative biosynthesis and to signaling. In filamentous fungi, NOX enzymes are involved in signaling cell differentiation, in particular in the formation of fruiting bodies. On the basis of bioinformatics analysis, until now it was believed that the genomes of unicellular fungi like Saccharomyces cerevisiae and Schizosaccharomyces pombe do not harbor genes coding for NOX enzymes. Nevertheless, the genome of S. cerevisiae contains nine ORFs showing sequence similarity to the catalytic subunits of mammalian NOX enzymes, only some of which have been functionally assigned as ferric reductases involved in iron ion transport. Here we show that one of the nine ORFs (YGL160W, AIM14) encodes a genuine NADPH oxidase, which is located in the endoplasmic reticulum (ER) and produces superoxide in a NADPH-dependent fashion. We renamed this ORF YNO1 (yeast NADPH oxidase 1). Overexpression of YNO1 causes YCA1-dependent apoptosis, whereas deletion of the gene makes cells less sensitive to apoptotic stimuli. Several independent lines of evidence point to regulation of the actin cytoskeleton by reactive oxygen species (ROS) produced by Yno1p.cell cycle | integral membrane reductase | wiskostatin | latrunculin R eactive oxygen species (ROS) have multiple roles in physiology and pathophysiology, in particular during aging and induction of programmed cell death. This includes also nonmitochondrial sources, besides the long-studied mitochondrially generated ROS. These findings can be viewed as important additions to the classical "free radical theory of aging" (1) and theories developed thereafter (2, 3).In higher organisms, among others, at least two major sources of superoxide other than mitochondria are known. On the one hand, xanthine oxidase, an enzyme in the catabolism of purines, which catalyses the oxidation of hypoxanthine to xanthine and to uric acid, produces superoxide (4). On the other hand, NADPH oxidases (NOX) catalyze the production of superoxide from oxygen and NADPH (5).The NADPH oxidase superfamily of membrane-located enzymes of higher cells has been known for a decade (for review, ref. 5). Whereas the human NOX2 was discovered early on, other NOX (Nox1/3/4/5) as well as dual oxidase (DUOX) (Duox1/2) enzymes (displaying two domains: a NADPH oxidase domain and a peroxidase domain) have been found relatively recently in human cells. The human NOX2 was discovered as a defense enzyme of neutrophils and macrophages, which produce a burst of superoxide (O 2 · − ) as a first line of defense against invading microorganisms. Although X-ray or NMR structure determinations are not available, we know from indirect evidence and bioinformatics that the catalytic subunit of the macrophage enzyme contains six transmembrane helices, is located in the plasma membrane, and produces superoxide in a vectorial ...

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Two NADPH oxidase isoforms are required for sexual reproduction and ascospore germination in the filamentous fungus Podospora anserina

Cited by 224 publications

References 40 publications

Trichoderma: sensing the environment for survival and dispersal

Trichoderma: sensing the environment for survival and dispersal

Mn(II) oxidation by an ascomycete fungus is linked to superoxide production during asexual reproduction

Yno1p/Aim14p, a NADPH-oxidase ortholog, controls extramitochondrial reactive oxygen species generation, apoptosis, and actin cable formation in yeast

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