Genome sequence of the model mushroom Schizophyllum commune

Ohm, Robin A.; Jong, Jan F. de; Lugones, Luis G.; Aerts, Andrea; Kothe, Erika; Stajich, Jason E.; Vries, Ronald P. de; Record, Éric; Levasseur, Anthony; Baker, Scott E.; Bartholomew, Kirk A.; Coutinho, Pedro M.; Erdmann, Susann; Fowler, Thomas J.; Gathman, Allen C.; Lombard, Vincent; Henrissat, Bernard; Knabe, Nicole; Kües, Ursula; Lilly, Walt W.; Lindquist, Erika; Lucas, Susan; Magnuson, Jon; Piumi, François; Raudaskoski, Marjatta; Salamov, Asaf; Schmutz, Jeremy; Schwarze, Francis W. M. R.; vanKuyk, Patricia A.; Horton, J. Stephen; Grigoriev, Igor V.; Wösten, Han A. B.

doi:10.1038/nbt.1643

Cited by 466 publications

(521 citation statements)

References 46 publications

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“…Chimeric lectins homologous to MOA are present in the basidiomycetes Polyporus squamosus (24) and Schizophyllum commune (25). In P. squamosus lectin, the catalytic triad and the four Asp residues taking part in Ca 2ϩ binding are conserved.…”

Section: Discussionmentioning

confidence: 99%

Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity

Wohlschlager¹,

Butschi

Zurfluh³

et al. 2011

Journal of Biological Chemistry

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Fruiting body lectins have been proposed to act as effector proteins in the defense of fungi against parasites and predators. The Marasmius oreades agglutinin (MOA) is a Gal␣1,3Gal/ GalNAc-specific lectin from the fairy ring mushroom that consists of an N-terminal ricin B-type lectin domain and a C-terminal dimerization domain. The latter domain shows structural similarity to catalytically active proteins, suggesting that, in addition to its carbohydrate-binding activity, MOA has an enzymatic function. Here, we demonstrate toxicity of MOA toward the model nematode Caenorhabditis elegans. This toxicity depends on binding of MOA to glycosphingolipids of the worm via its lectin domain. We show further that MOA has cysteine protease activity and demonstrate a critical role of this catalytic function in MOA-mediated nematotoxicity. The proteolytic activity of MOA was dependent on high Ca 2؉ concentrations and favored by slightly alkaline pH, suggesting that these conditions trigger activation of the toxin at the target location. Our results suggest that MOA is a fungal toxin with intriguing similarities to bacterial binary toxins and has a protective function against fungivorous soil nematodes.

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Section: Discussionmentioning

confidence: 99%

Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity

Wohlschlager¹,

Butschi

Zurfluh³

et al. 2011

Journal of Biological Chemistry

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show abstract

“…On the other hand, the homology of LSL to fruiting bodyspecific proteins of C. cinerea is restricted to the aerolysin domain (Plaza et al 2014). SCA and the C. cinerea homolog of LSL are differentially expressed in fruiting bodies compared to the vegetative mycelium in S. commune and in C. cinerea (Ohm et al 2010;Plaza et al 2014).…”

Section: β-Trefoil-type Chimerolectinsmentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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Fruiting bodies or sporocarps of dikaryotic (ascomycetous and basidiomycetous) fungi, commonly referred to as mushrooms, are often rich in entomotoxic and nematotoxic proteins that include lectins and protease inhibitors. These protein toxins are thought to act as effectors of an innate defense system of mushrooms against animal predators including fungivorous insects and nematodes. In this review, we summarize current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin-type lectins, beta-propeller-type lectins and beta-trefoil-type chimerolectins, as well as mycospin and mycocypin families of protease inhibitors. We also present an overview of the phylogenetic distribution of these proteins among a selection of fungal genomes and draw some conclusions about their evolution and physiological function. Finally, we present an outlook for future research directions in this field and their potential applications in medicine and crop protection.

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“…With roots as models for mating type genetics, both Ustilago maydis (Holliday 1961; Kronstad 2008) and Schizophyllum commune (Raper & Miles 1958; Ohm et al 2010) were characterised extensively in the classical genetics era and the role of these fungi as plant pathogens was not the driving force in their utilisation as model systems. Similarly, mating was studied in the saprophytic basidiomycete mushroom Coprinopsis cinerea and this system was ultimately exploited more for its synchronised meiosis than for its other features (Casselton & Kües 2007; Stajich et al 2010).…”

Section: Plant Pathogenic Fungi and Mushroomsmentioning

confidence: 99%

Diverse data supports the transition of filamentous fungal model organisms into the post-genomics era

McCluskey

Baker

2017

Mycology

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Filamentous fungi have been important as model organisms since the beginning of modern biological inquiry and have benefitted from open data since the earliest genetic maps were shared. From early origins in simple Mendelian genetics of mating types, parasexual genetics of colony colour, and the foundational demonstration of the segregation of a nutritional requirement, the contribution of research systems utilising filamentous fungi has spanned the biochemical genetics era, through the molecular genetics era, and now are at the very foundation of diverse omics approaches to research and development. Fungal model organisms have come from most major taxonomic groups although Ascomycete filamentous fungi have seen the most major sustained effort. In addition to the published material about filamentous fungi, shared molecular tools have found application in every area of fungal biology. Similarly, shared data has contributed to the success of model systems. The scale of data supporting research with filamentous fungi has grown by 10 to 12 orders of magnitude. From genetic to molecular maps, expression databases, and finally genome resources, the open and collaborative nature of the research communities has assured that the rising tide of data has lifted all of the research systems together.

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Genome sequence of the model mushroom Schizophyllum commune

Cited by 466 publications

References 46 publications

Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity

Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Diverse data supports the transition of filamentous fungal model organisms into the post-genomics era

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