Flammulina velutipes is a fungus with health and medicinal benefits that has been used for consumption and cultivation in East Asia. F. velutipes is also known to degrade lignocellulose and produce ethanol. The overlapping interests of mushroom production and wood bioconversion make F. velutipes an attractive new model for fungal wood related studies. Here, we present the complete sequence of the F. velutipes genome. This is the first sequenced genome for a commercially produced edible mushroom that also degrades wood. The 35.6-Mb genome contained 12,218 predicted protein-encoding genes and 287 tRNA genes assembled into 11 scaffolds corresponding with the 11 chromosomes of strain KACC42780. The 88.4-kb mitochondrial genome contained 35 genes. Well-developed wood degrading machinery with strong potential for lignin degradation (69 auxiliary activities, formerly FOLymes) and carbohydrate degradation (392 CAZymes), along with 58 alcohol dehydrogenase genes were highly expressed in the mycelium, demonstrating the potential application of this organism to bioethanol production. Thus, the newly uncovered wood degrading capacity and sequential nature of this process in F. velutipes, offer interesting possibilities for more detailed studies on either lignin or (hemi-) cellulose degradation in complex wood substrates. The mutual interest in wood degradation by the mushroom industry and (ligno-)cellulose biomass related industries further increase the significance of F. velutipes as a new model.

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Ganoderma applanatum is one of the most popular medicinal mushrooms due to the various biologically active components it produces. This study was conducted to obtain basic information regarding the mycelial culture conditions of Ganoderma applanatum. Based on the colony diameter and mycelial density, PDA, YMA and MCM media were suitable for the mycelial growth of the mushroom. The optimum temperature for mycelial growth was found to be 25~30℃. The optimum carbon and nitrogen sources were mannose and dextrin, respectively, and the optimum C/N ratio was 2 to 10 when 2% glucose was used. Other minor components required for the optimal growth included thiamine-HCl and biotin as vitamins, succinic acid and lactic acid as organic acids, and MgSO4·7H2O, KH2PO4 and NaCl as mineral salts.

A cDNA clone, PoMTP, encoding a putative metzincin family metalloprotease was isolated from the expressed sequence tags of a basidiomycete Pleurotus ostreatus. The 5'-end sequence of PoMTP was determined by the 5'-RACE method. Full-length cDNA sequence (1140 bp) of PoMTP contained a 870 bp open reading frame encoding a protein product of 290 amino acids in addition to a 99 bp of 5'-untranslated sequence and a 171 bp of 3'-untranslated sequence with a poly(A) tail. The deduced amino-acid sequences of PoMTP contained an extensive zinc-binding consensus sequence and a so-called Met-turn sequence which are typical for the metzincin family of metalloproteases, indicating that the PoMTP protein belongs to the metzincin metalloproteases. Four cysteine residues were also observed in the zinc-binding region of PoMTP amino-acid sequence, which are known to be important for the structure and the function of some subfamilies of the metzincins. Comparison of the PoMTP in sequence database showed no significant homology with functionally known metalloproteases of Armillaria mellea, Grifola frondosa, Lentinula edodes, Pleurotus ostreatus, Schizophyllum commune and Tricholoma saponaceum in mushroom. Northern blot and qunatitative RT-PCR analyses indicated the PoMTP mRNA to be abundant at primordial and fruit body stages, but scarce at the mycelial stage, suggesting that the PoMTP metalloprotease plays an important role in mushroom fruiting.