Hydrophobins DGH1, DGH2, and DGH3 in the Lichen-Forming Basidiomycete Dictyonema glabratum

Trembley, Marcella L.; Ringli, Christoph; Honegger, Rosmarie

doi:10.1006/fgbi.2001.1325

Cited by 35 publications

(33 citation statements)

References 42 publications

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“…Our result is especially striking considering that these are conspicuous macrolichens well known to the scientific community, having been used in numerous environmental, ecophysiological, chemical, and ultrastructural studies (10,(20)(21)(22)(23)(24)(25)(26)(27)(28). Until recently, it was believed that unrecognized species in lichenized Fungi would most likely be found among little-studied tropical microlichens, and it was predicted that the number of missing species is less than the number of already known species (6).…”

Section: Discussionmentioning

confidence: 77%

A single macrolichen constitutes hundreds of unrecognized species

Lücking

Dal-Forno

Sikaroodi

et al. 2014

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

154

121

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The number of Fungi is estimated at between 1.5 and 3 million. Lichenized species are thought to make up a comparatively small portion of this figure, with unrecognized species richness hidden among little-studied, tropical microlichens. Recent findings, however, suggest that some macrolichens contain a large number of unrecognized taxa, increasing known species richness by an order of magnitude or more. Here we report the existence of at least 126 species in what until recently was believed to be a single taxon: the basidiolichen fungus Dictyonema glabratum, also known as Cora pavonia. Notably, these species are not cryptic but morphologically distinct. A predictive model suggests an even larger number, with more than 400 species. These results call into question species concepts in presumably well-known macrolichens and demonstrate the need for accurately documenting such species richness, given the importance of these lichens in endangered ecosystems such as paramos and the alarming potential for species losses throughout the tropics.diversification | global diversity prediction | Hygrophoraceae

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Section: Discussionmentioning

confidence: 77%

A single macrolichen constitutes hundreds of unrecognized species

Lücking

Dal-Forno

Sikaroodi

et al. 2014

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

154

121

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“…Hydrophobin assemblies play many important roles in fungal biology, including reducing the surface tension of the growth medium to allow aerial hyphae to break through the air:liquid interface, 1 coating aerial structures and spores to render them hydrophobic and resistant to wetting, 2 and lining gas-exchange surfaces to prevent water logging. [3][4][5][6][7] They have also been shown to be of importance in pathogen:host interactions in plants 8 as well as in human infections. 9 Hydrophobins are considered to be one of the most surface-active molecules known.…”

Section: Introductionmentioning

confidence: 99%

Solution structure and interface‐driven self‐assembly of NC2, a new member of the Class II hydrophobin proteins

2013

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Hydrophobins are fungal proteins that self-assemble spontaneously to form amphipathic monolayers at hydrophobic:hydrophilic interfaces. Hydrophobin assemblies facilitate fungal transitions between wet and dry environments and interactions with plant and animal hosts. NC2 is a previously uncharacterized hydrophobin from Neurospora crassa. It is a highly surface active protein and is able to form protein layers on a water:air interface that stabilize air bubbles. On a hydrophobic substrate, NC2 forms layers consisting of an ordered network of protein molecules, which dramatically decrease the water contact angle. The solution structure and dynamics of NC2 have been determined using nuclear magnetic resonance spectroscopy. The structure of this protein displays the same core fold as observed in other hydrophobin structures determined to date, including the Class II hydrophobins HFBI and HFBII from Trichoderma reesei, but certain features illuminate the structural differences between Classes I and II hydrophobins and also highlight the variations between structures of Class II hydrophobin family members. The unique properties of hydrophobins have attracted much attention for biotechnology applications. The insights obtained through determining the structure, biophysical properties and assembly characteristics of NC2 will facilitate the development of hydrophobin-based applications.

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“…The scale bar represents 0.1 amino acid substitutions per position. GenBank accession numbers are shown as follows: Aa-Pri2/AAD41222 from Agrocybe aegerita (Santos and Labarere 1999); HYPA or ABH1/CAA61530 and HYPC or ABH2/CAA62332 from Agaricus bisporus (de Groot et al 1996, Lugones et al 1996; ABH3/CAA74940 from A. bisporus (Lugones et al 1998); CoH1/CAA71652 and CoH2/CAA71653 from Coprinus cinereus (Asgeirsdottir et al 1997); DGH1/CAC86002, DGH2/CAC86005 and DGH3/CAC86006 from Dictyonema glabratum (Trembley et al 2002); FVH1/BAB17622 from Flammulina velutipes (Ando et al 2001); Fv-HYD1/BAD08615 from F. velutipes (Yamada et al 2005); HYD1/AAL05426 from Tricholoma terreum (Mankel et al 2002); HYDPt-1/AAC49307, HYDPt-2/AAC49308 and HYDPt-3/AAC49306 from Pisolithus tinctorius (Tagu et al 1996); Le.HYD1/AAF61065 and Le.HYD2/AAF61066 from Lentinula edodes (Ng et al 2000); POH1/CAA12391, POH2/CAA12392 and POH3/CAA76494 from Pleurotus ostreatus ; FBH1/CAC95144 from P. ostreatus (Penas et al 1998); VMH1/CAD12829, VMH2/CAD12833 and VMH3/CAD12831 from P. ostreatus (Penas et al 2002); PNH1/BAB84545, PNH2/BAB84546 and PNH3/BAB84547 from Pholiota nameko (Tasaki et al 2004); SC1/CAA25366 and SC4/AAA33927 from Schizophyllum commune (Schuren and Wessels 1990); SC3/AAA96324 from S. commune (de Vocht et al 1998); from SC6/CAA07545 from S. commune (Wessels et al 1995). assembled at the interface between the mucilage and the gas phase. The assembled SC4 hydrophobin membrane provides air channels with a hydrophobic rodlet layer that prevents fruiting bodies from filling with water during cycles of drying and wetting (Wessels 1994, 1996, van Wetter 2000.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Pleurotus ostreatus fruiting body‐specific hydrophobin gene, Po.hyd

Shan

Wang

et al. 2007

J. Basic Microbiol.

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Hydrophobins are a family of small, moderately hydrophobic proteins with eight cysteine residues arranged in a conserved pattern. A full-length cDNA, designated Po.hyd, corresponding to a hydrophobin gene of Pleurotus ostreatus was obtained in our previous work. The Po.hyd gene contains a 333 bp open reading frame (ORF), which is interrupted by two typical classI introns. There was no consensus signal for a polyA tail detected in the 3'untranslated region. However, an analogous T- or TG-rich motif was observed that probably influence the formation of the mRNA 3' end. We assign the putative Po.HYD protein to the classI hydrophobins since its sequence arrangement and hydropathy pattern has a high consensus to other known class I hydrophobins. Northern analysis showed that the Po.hyd gene was abundantly expressed throughout the fruiting process (from primordium to mature fruiting body) but silenced during vegetative growth of the mycelium. Southern blot analysis showed Po.hyd to be a single copy gene in the genome of dikaryotic strain likely to locate at the same locus within the two parental genomes.

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Hydrophobins DGH1, DGH2, and DGH3 in the Lichen-Forming Basidiomycete Dictyonema glabratum

Cited by 35 publications

References 42 publications

A single macrolichen constitutes hundreds of unrecognized species

A single macrolichen constitutes hundreds of unrecognized species

Solution structure and interface‐driven self‐assembly of NC2, a new member of the Class II hydrophobin proteins

Characterization of a Pleurotus ostreatus fruiting body‐specific hydrophobin gene, Po.hyd

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