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Oxidative stress in fungi: its function in signal transduction, interaction with plant hosts, and lignocellulose degradation.

Breitenbach M, Weber M, Rinnerthaler M, Karl T, Breitenbach-Koller L - Biomolecules (2015)

Bottom Line: In this review article, we want to present an overview of oxidative stress in fungal cells in relation to signal transduction, interaction of fungi with plant hosts, and lignocellulose degradation.We will discuss external oxidative stress which may occur through the interaction with other microorganisms or plant hosts as well as internally generated oxidative stress, which can for instance originate from NADPH oxidases or "leaky" mitochondria and may be modulated by the peroxiredoxin system or by protein disulfide isomerases thus contributing to redox signaling.Analyzing redox signaling in fungi with the tools of molecular genetics is presently only in its beginning.

View Article: PubMed Central - PubMed

Affiliation: Department of Cell Biology, Division of Genetics, University of Salzburg, Salzburg 5020, Austria. Michael.BREITENBACH@sbg.ac.at.

ABSTRACT
In this review article, we want to present an overview of oxidative stress in fungal cells in relation to signal transduction, interaction of fungi with plant hosts, and lignocellulose degradation. We will discuss external oxidative stress which may occur through the interaction with other microorganisms or plant hosts as well as internally generated oxidative stress, which can for instance originate from NADPH oxidases or "leaky" mitochondria and may be modulated by the peroxiredoxin system or by protein disulfide isomerases thus contributing to redox signaling. Analyzing redox signaling in fungi with the tools of molecular genetics is presently only in its beginning. However, it is already clear that redox signaling in fungal cells often is linked to cell differentiation (like the formation of perithecia), virulence (in plant pathogens), hyphal growth and the successful passage through the stationary phase.

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Hypothetical structure of a typical NADPH oxidase. This structural model is based on bioinformatics, cell fractionation and biochemical data concerning the human Nox enyzmes (NOX1, 2, 3, and 4); no crystallographic or NMR structural data are available yet. Nox enzymes comprise typically about 500 amino acids and are exclusively located in lipid bylayer membranes, like the plasma membrane or the ER membrane. Large dots are highly conserved amino acids. The reaction center transferring a single electron to oxygen is the upper b-type heme in this scheme. The enzyme consists of six transmembrane helices. The two b-type hemes are coordinated with histidine residues between helices III and V. The enzyme contains binding sequences for NADPH as well as for FAD in its cytoplasmic tail (after Bedard and Krause 2007 [60]).
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biomolecules-05-00318-f003: Hypothetical structure of a typical NADPH oxidase. This structural model is based on bioinformatics, cell fractionation and biochemical data concerning the human Nox enyzmes (NOX1, 2, 3, and 4); no crystallographic or NMR structural data are available yet. Nox enzymes comprise typically about 500 amino acids and are exclusively located in lipid bylayer membranes, like the plasma membrane or the ER membrane. Large dots are highly conserved amino acids. The reaction center transferring a single electron to oxygen is the upper b-type heme in this scheme. The enzyme consists of six transmembrane helices. The two b-type hemes are coordinated with histidine residues between helices III and V. The enzyme contains binding sequences for NADPH as well as for FAD in its cytoplasmic tail (after Bedard and Krause 2007 [60]).

Mentions: NADPH oxidases are without exception located in biological membranes. They comprise 6 or 7 transmembrane helices, and produce superoxide in a vectorial way so that superoxide (in the example of the macrophage enzyme) is produced on the extracellular side of the plasma membrane and molecular oxygen and NADPH are consumed in the cytoplasm. The unique reaction catalyzed by NADPH oxidases is in need for three different cofactors: NADPH, FAD, and (two different) b-type cytochromes, as well as the substrate, dioxygen (Figure 3).The reaction equation can be summarized as: NADPH + 2O2 →NADP+ + 2O2− + H+.


Oxidative stress in fungi: its function in signal transduction, interaction with plant hosts, and lignocellulose degradation.

Breitenbach M, Weber M, Rinnerthaler M, Karl T, Breitenbach-Koller L - Biomolecules (2015)

Hypothetical structure of a typical NADPH oxidase. This structural model is based on bioinformatics, cell fractionation and biochemical data concerning the human Nox enyzmes (NOX1, 2, 3, and 4); no crystallographic or NMR structural data are available yet. Nox enzymes comprise typically about 500 amino acids and are exclusively located in lipid bylayer membranes, like the plasma membrane or the ER membrane. Large dots are highly conserved amino acids. The reaction center transferring a single electron to oxygen is the upper b-type heme in this scheme. The enzyme consists of six transmembrane helices. The two b-type hemes are coordinated with histidine residues between helices III and V. The enzyme contains binding sequences for NADPH as well as for FAD in its cytoplasmic tail (after Bedard and Krause 2007 [60]).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4496675&req=5

biomolecules-05-00318-f003: Hypothetical structure of a typical NADPH oxidase. This structural model is based on bioinformatics, cell fractionation and biochemical data concerning the human Nox enyzmes (NOX1, 2, 3, and 4); no crystallographic or NMR structural data are available yet. Nox enzymes comprise typically about 500 amino acids and are exclusively located in lipid bylayer membranes, like the plasma membrane or the ER membrane. Large dots are highly conserved amino acids. The reaction center transferring a single electron to oxygen is the upper b-type heme in this scheme. The enzyme consists of six transmembrane helices. The two b-type hemes are coordinated with histidine residues between helices III and V. The enzyme contains binding sequences for NADPH as well as for FAD in its cytoplasmic tail (after Bedard and Krause 2007 [60]).
Mentions: NADPH oxidases are without exception located in biological membranes. They comprise 6 or 7 transmembrane helices, and produce superoxide in a vectorial way so that superoxide (in the example of the macrophage enzyme) is produced on the extracellular side of the plasma membrane and molecular oxygen and NADPH are consumed in the cytoplasm. The unique reaction catalyzed by NADPH oxidases is in need for three different cofactors: NADPH, FAD, and (two different) b-type cytochromes, as well as the substrate, dioxygen (Figure 3).The reaction equation can be summarized as: NADPH + 2O2 →NADP+ + 2O2− + H+.

Bottom Line: In this review article, we want to present an overview of oxidative stress in fungal cells in relation to signal transduction, interaction of fungi with plant hosts, and lignocellulose degradation.We will discuss external oxidative stress which may occur through the interaction with other microorganisms or plant hosts as well as internally generated oxidative stress, which can for instance originate from NADPH oxidases or "leaky" mitochondria and may be modulated by the peroxiredoxin system or by protein disulfide isomerases thus contributing to redox signaling.Analyzing redox signaling in fungi with the tools of molecular genetics is presently only in its beginning.

View Article: PubMed Central - PubMed

Affiliation: Department of Cell Biology, Division of Genetics, University of Salzburg, Salzburg 5020, Austria. Michael.BREITENBACH@sbg.ac.at.

ABSTRACT
In this review article, we want to present an overview of oxidative stress in fungal cells in relation to signal transduction, interaction of fungi with plant hosts, and lignocellulose degradation. We will discuss external oxidative stress which may occur through the interaction with other microorganisms or plant hosts as well as internally generated oxidative stress, which can for instance originate from NADPH oxidases or "leaky" mitochondria and may be modulated by the peroxiredoxin system or by protein disulfide isomerases thus contributing to redox signaling. Analyzing redox signaling in fungi with the tools of molecular genetics is presently only in its beginning. However, it is already clear that redox signaling in fungal cells often is linked to cell differentiation (like the formation of perithecia), virulence (in plant pathogens), hyphal growth and the successful passage through the stationary phase.

Show MeSH