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PubMed1984

Properties of calcium-dependent regulatory proteins from fungi and yeast.

Calmodulins were isolated from vegetative mycelia of Basidiomycetes fungi, Agaricus campestris and Coprinus lagopus. These calmodulins showed similar mobilities to those of animal calmodulins on nondenaturing polyacrylamide gel electrophoresis in the presence or absence of Ca2+. The molecular weights of both calmodulins were determined to be 16,000. Agaricus calmodulin consisted of 148 amino acids including epsilon-N-trimethyllysine and cysteine. The UV-absorption spectrum showed the relatively high content of phenylalanine in Basidiomycetes calmodulins. The difference UV-absorption spectrum due to the blue shift by Ca2+ was observed. Both calmodulins activated muscle myosin light chain kinase and pea NAD+ kinase in a Ca2+-dependent manner, and the activities were inhibited by trifluoperazine or chlorpromazine. A calmodulin-like protein was partially purified from baker's yeast, Saccharomyces cerevisiae. However, detection of a calmodulin-like protein in prokaryotes was not successful.

Agaricales↗
PubMed1987

Basidiospore allergens: determination of optimal extraction methods.

Five methods were tested by RAST for allergen extraction from seven basidiospore species Armillaria tabescens, Chlorophyllum molybdites, Coprinus quadrifidus, Pleurotus ostreatus, Calvatia cyathiformis, Pisolithus tinctorius, and Scleroderma sp. With each basidiospore type, extracted allergen activity varied according to the method employed. In general, defatting of spores with ethyl ether, followed by homogenization in 0.125 M NH4HCO3 buffer, resulted in greatest allergen yield. In order to compare extracts from different isolates, batches of Pleurotus ostreatus spores obtained from different locations and over different time periods were analysed. Spores harvested from the same basidiomycete species in different areas varied in allergen (RAST) and protein (HPLC profile) content. The spores obtained from the same location over a 1-2 year period did not differ significantly. These results indicate that basidiospores can be stored for several years and that spore extracts from different locations can vary. These studies will help in the future to provide better characterized extracts for clinical studies.

Allergens↗
PubMed1996

Probing the aromatic-donor-binding site of horseradish peroxidase using site-directed mutagenesis and the suicide substrate phenylhydrazine.

The haem groups from two classes of site-directed mutants of horseradish peroxidase isoenzyme C (HRP-C) (distal haem pocket mutants, [H42L]HRP-C* and [R38K]-HRP-C* and peripheral-haem-access-channel mutants, [F142A]HRP-C* and [F143A]HRP-C*) were extracted and analysed by reverse-phase HPLC after phenylhydrazine-induced suicide inactivation. The relative abundance of the two covalently modified haems, C20-phenyl (delta-meso phenyl) and C18-hydroxymethyl haem, provided a sensitive topological probe for changes induced in the protein architecture in the vicinity of the haem active site and substrate-access channel. Although differing considerably in their efficiency as peroxidases ([H42L]HRP-C* exhibited only approximately 0.03% of the peroxidase activity of wild type), the variants studied gave rise to a modification pattern typical of an exposed haem edge thereby strengthening the argument that it is the overall protein topology rather than the intrinsic catalytic activity of the active site that determines the sites of covalent haem modification. Mutants which showed impaired ability to bind the aromatic donor benzhydroxamic acid were less readily modified by the phenyl radical at the haem C18-methyl position although the level of arylation at the haem C20 position remained remarkable constant. Our findings suggest that the overall efficacy of haem modification catalysed by HRP-C during turnover with phenylhydrazine and its vulnerability towards inactivation are related to its general ability to bind aromatic donor molecules. Results from phenylhydrazine treatment of HRP-C wild-type and mutant variants were compared with those obtained for Coprinus cinereus peroxidase, an enzyme which from its structure is known to have a remarkably open access channel to the haem edge. We show evidence that C. cinereus peroxidase is able to bind benzhydroxamic acid, albeit with a relatively high Kd (Kd 3.7 mM), a probe for aromatic-donor binding. We suggest reasons why phenylhydrazine-treated C. cinereus peroxidase was more resistant to haem modification and phenyl-radical-based inactivation than HRP-C.

Binding Sites↗
PubMed1997

Fatal pulmonary infection caused by the basidiomycete Hormographiella aspergillata.

A fatal case of a pulmonary infection caused by Hormographiella aspergillata, the anamorph of the mushroom Coprinus cinereus, is reported for a patient receiving treatment for a second relapse of acute lymphoblastic leukemia. The filamentous basidiomycete was identified with restriction fragment length polymorphism patterns of PCR-amplified internally transcribed spacers and small subunit ribosomal DNA with four restriction enzymes. The patient failed to respond to treatment with amphotericin B and itraconazole. The fungus was cultured from the lungs at autopsy: the MIC of amphotericin B for the fungus was low (0.5 mg/liter), and that of itraconazole was high (8 mg/liter).

Adult↗
PubMedDate not supplied

A low molecular weight peptide from snow mold with epitopic homology to the winter flounder antifreeze protein.

Evidence for a small size protein (ca. 3500 kDa) exhibiting epitopic homology to the Atlantic winter flounder antifreeze protein (AFP) is found in the snow molds Coprinus psychromorbidus, Myriosclerotinia borealis, and Typhula incarnata. The protein shows strong cross-reactivity with antisera specific for the flounder AFP. Preliminary studies suggest that the protein is synthesized in response to lowering the culture temperature, and that it is membrane associated and, therefore, may function in an analogous capacity to the fish AFP. Also, the protein is shown to have antifreeze properties as determined by nuclear magnetic resonance microimaging experiments.

Agaricales↗
PubMed2000

Production of cellulases and xylanases by low-temperature basidiomycetes.

Three of four isolates, representing phylogenetically distinct groupings of low-temperature basidiomycetes (LTB), were capable of utilizing wheat straw, and to a lesser extent conifer wood at 15 degrees C. A cottony snow mould LTB (LRS 013) and a fruit rot LTB (LRS 241) grown on straw significantly degraded filter paper, carboxymethylcellulose (CMC), p-nitrophenyl beta-glucopyranoside (i.e., beta-glucosidases), and xylan. Enzymes produced by Coprinus psychromorbidus (LRS 067) were limited to xylanases from straw and wood and beta-glucosidases from wood. A sclerotia-forming LTB (LRS 131) exhibited poor growth on both substrates, and did not produce detectable quantities of extracellular enzymes. None of the LTB isolates tested degraded avicel. The temperature optima of CMCases and xylanases in the filtrates from the straw medium ranged from 25 degrees C to 55 degrees C, and with the exception of LRS 067, significant activity was observed at 5 degrees C. Two cellulases (25 and 31 kDa) and two xylanases (24 and 34 kDa) were observed on zymograms for LRS 013 and 241. Reduction of enzymes with 2-mercaptoethanol adversely affected their activity on zymograms, and an additional cellulase band was observed for non-reduced samples. This study indicates that LTB produce an array of cellulolytic and xylanolytic enzymes, and that some of these enzymes possess low-temperature optima which may facilitate degradation of plant fibre under low-temperature conditions.

Basidiomycota↗
PubMed2001

Dioxygen reactivity of laccase: dependence on laccase source, pH, and anion inhibition.

A study was carried out on the dioxygen reactivity of the laccases from Trametes villosa, Rhizoctonia solani, Myceliophthora thermophila, Scytalidium thermophilum, and Coprinus cinereus. At pH 5.5, these laccases showed an apparently constant Km (about 20-50 microM) for O2 with either 2,2'-azinobis (3-ethylbenzothiazoline-6-sulfonic acid) or methyl syringate as the reducing substrate, in contrast to the kcat, which varied up to 100-fold. O2 reactivity of the Trametes and Myceliophthora laccases was also studied at various pH and NaF concentrations. The apparent Km of Trametes and Myceliophthora laccases varied only slightly when pH changed from 3.0 to 8.0 or when the laccases were inhibited by F- at pH 5.5, although the apparent kcat were more significantly affected by both factors. The dependence of the apparent Km on the source of laccase, pH, and F- inhibition suggested that the fungal laccases might have a conserved O2 pocket and that the F- or OH- inhibition might affect the O2 reduction step (kcat) more than the O2 binding step (Km) under steady-state conditions.

Anions↗
PubMed2006

Evaluation of agrobacterium-mediated transformation of Agaricus bisporus using a range of promoters linked to hygromycin resistance.

There is interest in establishing genetic modification technologies for the cultivated mushroom Agaricus bisporus, both for improved crop characteristics and for molecular pharming. For these methods to be successful, it is necessary to establish a set of transformation systems that include robust and reliable vectors for gene manipulation. In this article, we report the evaluation of a series of promoters for driving expression of the Escherichia coli hph gene encoding hygromycin phosphotransferase. This was achieved using the Aspergillus nidulans gpdA and the A. bisporus gpdII and trp2 promoters. The Coprinus cinereus beta-tubulin promoter gave contrasting results depending on the size of promoter used, with a 393-bp region being effective, whereas the longer 453-bp fragment failed to yield any hygromycin-resistant transformants. The C. cinereus trp1 and the A. bisporus lcc1 promoters both failed to yield transformants. We also show that transformation efficiency may be improved by careful selection of both appropriate Agrobacterium strains, with AGL-1 yielding more than LBA1126 and by the choice of the binary vectors used to mobilize the DNA, with pCAMBIA vectors appearing to be more efficient than either pBIN19- or pGREEN-based systems.

Agaricus↗
PubMed1991

Metabolic products of microorganisms. 258. Enzymatic bromination of nikkomycin Z.

Two brominated nikkomycins were produced by enzymatic halogenation of nikkomycin Z in the presence of a nonheme bromoperoxidase isolated from Streptomyces aureofaciens Tü 24. The monobrominated and dibrominated nikkomycin Z derivatives were substituted at the hydroxypyridyl moiety of the N-terminal amino acid of nikkomycin Z at position C-6"' (ZBr) or C-4"' and C-6"' (ZBr2). The brominated nikkomycin Z derivatives had a decreased affinity to chitin synthase of Coprinus cinereus as compared to nikkomycin Z and exhibited a low inhibitory activity towards various fungi and yeasts.

Aminoglycosides↗
PubMed1994

Gravitational biology of mushrooms: a flow-chart approach to characterising processes and mechanisms.

Flow charts are presented which systematise recently published work on gravitropic responses of the mushroom stipe of Coprinus cinereus. The hypothetical model represented by the charts suggests that the meiotic division is a pivotal point in the gravitational biology of the mushroom fruit body. The unilateral gravity vector seems to be required for formation of the tissues in which meiosis normally occurs, and stipes become gravitropically competent only after onset of meiosis. The gravitropism flow-chart also indicates that two signals emanate from the upper regions of the stipe, one promotes the process of gravitropic bending, and is followed by a second signal which compensates for excess bending and adjusts the stipe apex to the vertical. Formalisation of the various observations into flow-charts, even though comparatively simple at the moment, facilitates comparison with other species and concentrates attention on aspects requiring further experimental analysis.

Calcium↗
PubMedDate not supplied

[Effect of cocultivating fungal species on the degradation of lignocellulose residues].

The degradation potential of Phanerochaete sordida, Trametes trogii, Coprinus truncorum and Paecilomyces sp. upon yard wastes was evaluated. The species had been inoculated individually or in pairs formed by P. sordida and Paecilomyces sp., T. trogii and Paecilomyces sp., and C. truncorum and Paecilomyces sp. The highest level of endoxilanase activity was produced by P. sordida growing alone, during day 21 (1.09 U/g of dry material), but in P. sordida and Paecilomyces sp. cultures, the detected activity did not overcome 0.27 U/g of dry material during the whole experiment. T. trogii showed maximum activity on day 14 (0.78 U/g of dry material), but in T. trogii and Paecilomyces sp. cultures, the values increased until day 21 (1.07 U/g of dry material). P. sordida endocellulase activity reached its maximum on day 28 (0.08 U/g of dry material), but in P. sordida and Paecilomyces sp. cultures, this activity increased during the whole experiment (0.04 U/g of dry material). The major weight loss was found in P. sordida (27.6%). The possible beneficial effect of co-culture in yard wastes biodegradation is discussed.

Basidiomycota↗
PubMed1994

High concentrations of mannitol in the shiitake mushroom Lentinula edodes.

A quantitative analysis of mannitol, using gas-liquid chromatography (GLC), was carried out in the various tissues of Lentinula edodes (Berk.) Pegler in comparison with Agaricus bisporus (Lge) Imb. and Coprinus cinereus (Schaeff.: Fr.) S. F. Gray. Mycelia of L. edodes had a low level of mannitol (ca 1% on a dry wt basis) compared with the fruit body stipe and pileus (20-30%). The highest level of mannitol was observed in the pileus of A. bisporus (close to 50%). These observations of similar levels of accumulation of mannitol suggest that glucose catabolism in L. edodes and A. bisporus are similar. No mannitol was detectable in the pileus of C. cinereus.

Agaricus↗
PubMed1999

Molecular cloning of homologs of RAS and RHO1 genes from Cryptococcus neoformans.

We cloned and sequenced homologs of RAS(CnRAS) and RHO1(CnRHO1) genes from Cryptococcus neoformans. The proteins encoded by the CnRAS and CnRHO1 genes contained 216 and 197 amino acids, respectively. The deduced amino acid sequence of the CnRAS gene shared a high degree of sequence identity with the Ras proteins in other fungal species: Coprinus cinereus(76%), Lentinula edodes(74%), Saccharomyces cerevisiae RAS2(72%), and Schizosaccharomyces pombe(68%). The deduced amino acid sequence of the CnRHO1 gene shared a high degree of sequence identity with the Rho1 proteins in other fungal species: Candida albicans(78%), S. pombe(77%) and S. cerevisiae(76%). The deduced proteins contained GTP-binding and GTP-hydrolysis domains, and the prenylation site that are conserved among the small G protein superfamily. The synthetic peptides that contained the C-terminal amino acid sequence of the CnRas and CnRho1 proteins were geranylgeranylated.

Amino Acid Sequence↗
PubMed2003

Combined sequence and structure analysis of the fungal laccase family.

Plant and fungal laccases belong to the family of multi-copper oxidases and show much broader substrate specificity than other members of the family. Laccases have consequently been of interest for potential industrial applications. We have analyzed the essential sequence features of fungal laccases based on multiple sequence alignments of more than 100 laccases. This has resulted in identification of a set of four ungapped sequence regions, L1-L4, as the overall signature sequences that can be used to identify the laccases, distinguishing them within the broader class of multi-copper oxidases. The 12 amino acid residues in the enzymes serving as the copper ligands are housed within these four identified conserved regions, of which L2 and L4 conform to the earlier reported copper signature sequences of multi-copper oxidases while L1 and L3 are distinctive to the laccases. The mapping of regions L1-L4 on to the three-dimensional structure of the Coprinus cinerius laccase indicates that many of the non-copper-ligating residues of the conserved regions could be critical in maintaining a specific, more or less C-2 symmetric, protein conformational motif characterizing the active site apparatus of the enzymes. The observed intraprotein homologies between L1 and L3 and between L2 and L4 at both the structure and the sequence levels suggest that the quasi C-2 symmetric active site conformational motif may have arisen from a structural duplication event that neither the sequence homology analysis nor the structure homology analysis alone would have unraveled. Although the sequence and structure homology is not detectable in the rest of the protein, the relative orientation of region L1 with L2 is similar to that of L3 with L4. The structure duplication of first-shell and second-shell residues has become cryptic because the intraprotein sequence homology noticeable for a given laccase becomes significant only after comparing the conservation pattern in several fungal laccases. The identified motifs, L1-L4, can be useful in searching the newly sequenced genomes for putative laccase enzymes.

Amino Acid Sequence↗
PubMed1993

Effect of phenol on the mycelial growth and fructification in some of basidiomycetous fungi.

Cometabolic growth studies with phenol were undertaken to screen 32 strains of white and brown rot fungi. All the cultures studied grew well up to 4 mM of phenol on Czapekdox agar except Agaricus bisporus (white button mushroom) and Pleurotus cystidiosus. Most of them could grow even up to 6 mM of phenol. Phenol induced a brown pigmentation of the culture medium. P. flabellatus and P. pulmonarius metabolized 67 and 64 mg/l phenol in 10 days. Studies have indicated that phenol (0.1 to 1.0 mM) incorporated in malt-extract agar has no inhibitory effect on fruitbody formation. Preliminary studies indicate that soaking of wheat straw with phenol solution up to 1600 mg/l give better mycelial growth and fructification of P. cornucopiae, P. ostreatus Z-15 and Calocybe indica than water soaked. Soaking of wheat straw in phenol inhibited the growth of common competitor weed fungi like Stachybotrys sp. and Coprinus sp.

Basidiomycota↗
PubMed2003

Isolation of vulgin, a new antifungal polypeptide with mitogenic activity from the pinto bean.

An antifungal polypeptide bearing an N-termnial sequence with some homology to chitinases was purified from an extract of pinto beans. The polypeptide, designated vulgin, exerted antifungal activity toward Mycosphaerella arachidicola, Coprinus cornatus, Fusarium oxysporum and Botrytis cinerea. Vulgin inhibited translation in a rabbit reticulocyte lysate system with an IC50 of 4.3 microM and HIV-1 reverse transcriptase activity with an IC50 of 58 microM. Vulgin stimulated in vitro incorporation of methyl [3H] thymidine into mouse splenocytes.

Amino Acid Sequence↗
PubMed1997

Further studies on the inactivation by sodium azide of lignin peroxidase from Phanerochaete chrysosporium.

Azide ion is a mechanism-based inactivator of horseradish peroxidase [Ortiz de Montellano et al. (1988) Biochemistry 27, 5470-5476] and the peroxidase from the coprophilic fungus Coprinus macrorhizus [DePillis and Ortiz de Montellano (1989) Biochemistry 28, 7947-7952]. These peroxidases mediate the one-electron oxidation of azide ion-forming azidyl radical. Inactivation of these enzymes is caused by covalent modification of the heme prosthetic groups by azidyl radical. Lignin peroxidases from the wood-rotting fungus Phanerochaete chrysosporium are also inactivated when they catalyze oxidation of azide ion [Tuisel et al. (1991) Arch. Biochem. Biophys. 288, 456-462; DePillis et al. (1990) Arch. Biochem. Biophys. 280, 217-223]. Following inactivation of horseradish peroxidase and the peroxidase from C. macrorhizus substantial amounts of azidyl-heme adducts have been found. Only trace amounts of such adducts have been found following azide-mediated inactivation of lignin peroxidase. Nevertheless, we have shown that during oxidation of azide by lignin peroxidase H8 destruction of heme occurred and a substantial fraction of the enzyme is irreversibly inactivated. However, the rest of the enzyme forms a relatively stable ferrous-nitric oxide (NO) complex. Although this complex appears to be an inactivated form of the enzyme, we have shown that, when present as the ferrous-NO complex, the enzyme is actually protected from inactivation. The lignin peroxidase ferrous-NO complex reverts slowly (t1/2 = 6.3 x 10(3) s) to the ferric form. Reversion is accelerated if the complex is chromatographed on a PD-10 (Sephadex G-25) column or if veratryl alcohol is added. If azide and hydrogen peroxide (a required cosubstrate) are present (or added), the enzyme undergoes another cycle of catalysis and further inactivation. A detailed reaction mechanism is proposed that is consistent with our experimental observations, the chemistry of azide, and our current understanding of peroxidases.

Azides↗
PubMed2000

Quinqueginsin, a novel protein with anti-human immunodeficiency virus, antifungal, ribonuclease and cell-free translation-inhibitory activities from American ginseng roots.

A homodimeric protein designated quinqueginsin, with a molecular weight of 53 kDa, has been isolated from the roots of American ginseng Panax quinquefolium. It was unadsorbed on DEAE cellulose in low ionic strength and neutral pH, and adsorbed on Affigel blue gel and SP-Sepharose under similar conditions. Its N-terminal sequence bore similarity to those of plant ribosome inactivating proteins and fungal ribonucleases. The protein displayed a variety of biological activities. It possessed ribonucleolytic activity toward yeast tRNA and specific activity toward poly C. It inhibited cell-free translation in a rabbit reticulocyte lysate system with an IC(50) of 0.26 nM, and exerted antifungal action against Fusarium oxysporum, Rhizoctonia solani, and Coprinus comatus. An inhibitory action was expressed toward human immunodeficiency virus-1 reverse transcriptase. This action was potentiated after chemical modification with succinic anhydride.

Amino Acid Sequence↗