Browse
Submit Data
Databases
API
Help

Dataset Information

10 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Taxonomic Evaluation of a Bioherbicidal Isolate of Albifimbria verrucaria, Formerly Myrothecium verrucaria.

ABSTRACT: The fungal genus Myrothecium was once polyphyletic but a recent reconsideration of the family Stachybotryaceae spilt it into several genera. The ex-neotype specimen of the species Myrothecium verrucaria is now recognized as Albifimbria verrucaria. The well-studied plant pathogen and candidate bioherbicide CABI-IMI 368023, previously identified as M. verrucaria, was analyzed morphologically and genetically and found to be most consistently aligned with the other representatives of A. verrucaria.

SUBMITTER: Weaver MA

PROVIDER: S-EPMC8465294 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Similar Datasets

THE FRACTIONATION OF MYROTHECIUM VERRUCARIA CELLULASE BY GEL FILTRATION.

Project description:1. Culture filtrates from Myrothecium verrucaria have been fractionated by gel filtration on Sephadex G-75 to give three major cellulolytic components with molecular weights of about 55000, 30000 and 5300. 2. The middle component has the bulk (90%) of the total carboxymethylcellulase activity and is little affected by exposure to cotton. The other two, which are mainly responsible for the activity of the filtrate towards cotton, are removed or deactivated by exposure to it. These observations accord with the previously reported behaviour of the whole culture filtrate. There is no evidence for interconversion of, or synergism between, these components. 3. Temperature control during gel filtration is necessary for reproducible results at high resolution. The effect of a change in temperature has been explained in terms of changes in the degree of swelling of the gel particles.

| S-EPMC1206591 | biostudies-other

X-ray analysis of bilirubin oxidase from Myrothecium verrucaria at 2.3 A resolution using a twinned crystal.

Project description:Bilirubin oxidase (BOD), a multicopper oxidase found in Myrothecium verrucaria, catalyzes the oxidation of bilirubin to biliverdin. Oxygen is the electron acceptor and is reduced to water. BOD is used for diagnostic analysis of bilirubin in serum and has attracted considerable attention as an enzymatic catalyst for the cathode of biofuel cells that work under neutral conditions. Here, the crystal structure of BOD is reported for the first time. Blue bipyramid-shaped crystals of BOD obtained in 2-methyl-2,4-pentanediol (MPD) and ammonium sulfate solution were merohedrally twinned in space group P6(3). Structure determination was achieved by the single anomalous diffraction (SAD) method using the anomalous diffraction of Cu atoms and synchrotron radiation and twin refinement was performed in the resolution range 33-2.3 A. The overall organization of BOD is almost the same as that of other multicopper oxidases: the protein is folded into three domains and a total of four copper-binding sites are found in domains 1 and 3. Although the four copper-binding sites were almost identical to those of other multicopper oxidases, the hydrophilic Asn residue (at the same position as a hydrophobic residue such as Leu in other multicopper oxidases) very close to the type I copper might contribute to the characteristically high redox potential of BOD.

| S-EPMC2898457 | biostudies-literature

Ribosomal resistance to the 12,13-epoxytrichothecene antibiotics in the producing organism Myrothecium verrucaria.

Project description:An extract of Myrothecium verrucaria, a fungus which produces a range of 12,13-epoxytrichothecene toxins, was found to be resistant to T-2 toxin, one of its products. The epoxytrichothecenes are inhibitors of eukaryotic protein synthesis and normally bind to the 60S ribosomal subunit so as to inhibit peptidyltransferase activity. Ribosomes from M. verrucaria contain 60S subunits which are not subject to inhibition by T-2 toxin and are also resistant to certain other drugs such as anisomycin and homoharringtonine, but not sparsomycin or cycloheximide.

| S-EPMC1162157 | biostudies-other

Genome sequences of Rhizopogon roseolus, Mariannaea elegans, Myrothecium verrucaria, and Sphaerostilbella broomeana and the identification of biosynthetic gene clusters for fungal peptide natural products.

Project description:In recent years, a variety of fungal cyclic peptides with interesting bioactivities have been discovered. For many of these peptides, the biosynthetic pathways are unknown and their elucidation often holds surprises. The cyclic and backbone N-methylated omphalotins from Omphalotus olearius were recently shown to constitute a novel class (borosins) of ribosomally synthesized and posttranslationally modified peptides, members of which are produced by many fungi, including species of the genus Rhizopogon. Other recently discovered fungal peptide macrocycles include the mariannamides from Mariannaea elegans and the backbone N-methylated verrucamides and broomeanamides from Myrothecium verrucaria and Sphaerostilbella broomeana, respectively. Here, we present draft genome sequences of four fungal species Rhizopogon roseolus, Mariannaea elegans, Myrothecium verrucaria, and Sphaerostilbella broomeana. We screened these genomes for precursor proteins or gene clusters involved in the mariannamide, verrucamide, and broomeanamide biosynthesis including a general screen for borosin-producing precursor proteins. While our genomic screen for potential ribosomally synthesized and posttranslationally modified peptide precursor proteins of mariannamides, verrucamides, broomeanamides, and borosins remained unsuccessful, antiSMASH predicted nonribosomal peptide synthase gene clusters that may be responsible for the biosynthesis of mariannamides, verrucamides, and broomeanamides. In M. verrucaria, our antiSMASH search led to a putative NRPS gene cluster with a predicted peptide product of 20 amino acids, including multiple nonproteinogenic isovalines. This cluster likely encodes a member of the peptaibols, an antimicrobial class of peptides previously isolated primarily from the Genus Trichoderma. The nonribosomal peptide synthase gene clusters discovered in our screenings are promising candidates for future research.

| S-EPMC9258550 | biostudies-literature

Production of Laccase by a New Myrothecium verrucaria MD-R-16 Isolated from Pigeon Pea [Cajanus cajan (L.) Millsp.] and its Application on Dye Decolorization.

Project description:The present study was conducted to screen a laccase-producing fungal endophyte, optimize fermentation conditions, and evaluate the decolorization ability of the laccase. A new fungal endophyte capable of laccase-producing was firstly isolated from pigeon pea and identified as Myrothecium verrucaria based on a ITS-rRNA sequences analysis. Meanwhile, various fermentation parameters on the laccase production were optimized via response surface methodology (RSM). The optimal fermentation conditions were a fermentation time of five days, temperature 30 °C and pH 6.22. Laccase activity reached 16.52 ± 0.18 U/mL under the above conditions. Furthermore, the laccase showed effective decolorization capability toward synthetic dyes (Congo red, Methyl orange, Methyl red, and Crystal violet) in the presence of the redox mediator ABTS, with more than 70% of dyes decolorizing after 24 h of incubation. Additionally, the activity of laccase was relatively stable with pH (4.5-6.5) and a temperature range of 35-55 °C. Therefore, the high laccase production of the strain and the new fungal laccase could provide a promising alterative approach for industrial and environmental applications.

| S-EPMC6154323 | biostudies-literature

Isolation and properties of a nitrile hydratase from the soil fungus Myrothecium verrucaria that is highly specific for the fertilizer cyanamide and cloning of its gene.

Project description:A protein was purified from crude extracts of the soil fungus Myrothecium verrucaria by gel filtration and hydrophobic chromatography to homogeneity; this protein catalyzed the stoichiometric hydration of the fertilizer cyanamide to urea with high substrate specificity. This cyanamide hydratase (urea hydro-lyase; EC 4.2.1.69) contained zinc and consisted of six identical subunits with Mr = 27,700. It was partially sequenced. The protein was detectable only when the fungus was grown on cyanamide as the sole nitrogen source. Genomic DNA from the fungus was cloned, and the gene encoding the enzyme was mapped with an oligonucleotide probe derived from the amino acid sequence within a 25,800-base-pair DNA region. The subunit of the enzyme is encoded by a 795-base-pair DNA sequence containing a 63-base-pair intron. A cDNA clone containing the intronless gene with an open reading frame encoding a sequence of 244 amino acids expressed the enzyme in active form in Escherichia coli with excellent yield.

| S-EPMC51638 | biostudies-other

Albifimbria verrucaria

Project description:Albifimbria verrucaria overview

| PRJNA762414 | ENA

Myrothecium inundatum

Project description:Myrothecium inundatum overview

| PRJNA259256 | ENA

Genome sequences of Rhizopogon roseolus, Mariannaea elegans, Myrothecium verrucaria and Sphaerostilbella broomeana

Project description:We present draft genome sequences of the four fungal species Rhizopogon roseolus, Mariannaea elegans, Myrothecium verrucaria and Sphaerostilbella broomeana

| PRJEB50709 | ENA

Polyketides from the halotolerant fungus Myrothecium sp. GS-17.

Project description:Two new polyketides, myrothecol (1) and 5-hydroxy-3-methyl-4-(1-hydroxylethyl)-furan-2(5H)-one (2), were isolated from the fermentation broth of the halotolerant fungus Myrothecium sp. GS-17 along with three known compounds, 5-hydroxyl-3-[(1S)-1-hydroxyethyl]-4-methylfuran-2(5H)-one (3), 3,5-dimethyl-4- hydroxylmethyl-5-methoxyfuran-2(5H)-one (4), and 3,5-dimethyl-4-hydroxymethyl-5- hydroxyfuran-2(5H)-one (5). Compound 1 is the first natural occurring polyketide with a unique furylisobenzofuran skeleton. The structures of these compounds were established via extensive spectroscopic analyses including 1D-, 2D-NMR, HRESI-MS, and crystal X-ray diffraction analysis.

| S-EPMC6270343 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data