ArticlePloS one2012
Genomic clustering and homology between HET-S and the NWD2 STAND protein in various fungal genomes.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 86 citations in OpenAlex.
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- Harnessing deep learning for proteome-scale detection of amyloid signaling motifs.Bioinformatics (Oxford, England) · 2025Article
- Genomic organization, domain assortments, and nucleotide-binding domain diversity of NLR proteins in Sordariales fungi.PLoS genetics · 2025Article
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- Starship giant transposable elements cluster by host taxonomy using k-mer-based phylogenetics.G3 (Bethesda, Md.) · 2025Article
- Deep orange gene editing triggers temperature-sensitive lethal phenotypes in Ceratitis capitata.BMC biotechnology · 2024Article
- A Story Between s and S: [Het-s] Prion of the FungusMycobiology · 2024Review
- The phenomenon of strain degeneration in biotechnologically relevant fungi.Applied microbiology and biotechnology · 2023Review
- Emergence of the fungal immune system.iScience · 2023Review
- Exploring a diverse world of effector domains and amyloid signaling motifs in fungal NLR proteins.PLoS computational biology · 2022Article
- Homing in on gasdermins: How fungi regulate cell death.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Fungal gasdermin-like proteins are controlled by proteolytic cleavage.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Comparative Genomics Reveals Evolutionary Traits, Mating Strategies, and Pathogenicity-Related Genes Variation ofFrontiers in microbiology · 2022Article
- Genome Analysis of the Broad Host Range NecrotrophFrontiers in plant science · 2022Article
- Molecular Mechanisms and Evolutionary Consequences of Spore Killers in Ascomycetes.Microbiology and molecular biology reviews : MMBR · 2021Review
- The expanding scope of amyloid signalling.Prion · 2021Article
- Searching for universal model of amyloid signaling motifs using probabilistic context-free grammars.BMC bioinformatics · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPrions are infectious proteins propagating as self-perpetuating amyloid polymers. The [Het-s] prion of Podospora anserina is involved in a cell death process associated with non-self recognition. The prion forming domain (PFD) of HET-s adopts a β-solenoid amyloid structure characterized by the two fold repetition of an elementary triangular motif. [Het-s] induces cell death when interacting with HET-S, an allelic variant of HET-s. When templated by [Het-s], HET-S undergoes a trans-conformation, relocates to the cell membrane and induces toxicity. METHODOLOGY/PRINCIPAL
findingsHere, comparing HET-s homologs from different species, we devise a consensus for the HET-s elementary triangular motif. We use this motif to screen genomic databases and find a match to the N-terminus of NWD2, a STAND protein, encoded by the gene immediately adjacent to het-S. STAND proteins are signal transducing ATPases which undergo ligand-induced oligomerisation. Homology modelling predicts that the NWD2 N-terminal region adopts a HET-s-like fold. We propose that upon NWD2 oligomerisation, these N-terminal extensions adopt the β-solenoid fold and template HET-S to adopt the amyloid fold and trigger toxicity. We extend this model to a putative prion, the σ infectious element in Nectria haematococca, because the s locus controlling propagation of σ also encodes a STAND protein and displays analogous features. Comparative genomic analyses indicate evolutionary conservation of these STAND/prion-like gene pairs, identify a number of novel prion candidates and define, in addition to the HET-s PFD motif, two distinct, novel putative PFD-like motifs. CONCLUSIONS/SIGNIFICANCE: We suggest the existence, in the fungal kingdom, of a widespread and evolutionarily conserved mode of signal transduction based on the transmission of an amyloid-fold from a NOD-like STAND receptor protein to an effector protein.
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