The Sc7/Sc14 gene family of Schizophyllum commune codes for extracellular proteins specifically expressed during fruit-body formation

Schuren, Frank; Ásgeirsdóttir, Sigrídur A.; Kothe, Erika; Scheer, José M. J.; Wessels, J. G. H.

doi:10.1099/00221287-139-9-2083

Cited by 60 publications

(43 citation statements)

References 21 publications

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“…The Sc7 and Sc14 genes from Schizophyllum commune are specifically expressed in the dikaryon during fruiting. The Sc7p protein appears to be secreted and has been suggested to play a role in interaction between the dikaryotic hyphae leading to formation of pseudo-parenchymous tissue [67]. Sequences from Saccharomyces cere isiae were determined in the framework of the EU BIOTECH project for sequencing the yeast genome.…”

Section: Comparative Analysis Of Pr-1 Type Proteinsmentioning

confidence: 99%

The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins

Loon

Strien

1999

Physiological and Molecular Plant Pathology

1,646

929

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Section: Comparative Analysis Of Pr-1 Type Proteinsmentioning

confidence: 99%

The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins

Loon

Strien

1999

Physiological and Molecular Plant Pathology

1,646

929

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“…Over sixty-five proteins with high sequence homology to the plant PR-1 family have now been identified in the animal (invertebrates and vertebrates, including humans) and fungal kingdoms. Proteins include the human brain tumor PR proteins GliPR (17) and RTVP-1 (18), mammalian Tpx-1, testis-specific protein (19), helothermine, from lizard venom (20), antigen 5 from Vespula vilgaris venom (21), and proteins from fungi (Saccharomyces, Schizophylum) (22). Sequence alignment of PR proteins reveals a highly conserved core of amino acids (Fig.…”

Section: Fig 3 Sequence Alignment Of Representative Pathogenesis-rementioning

confidence: 99%

Isolation and Characterization of a Cone Snail Protease with Homology to CRISP Proteins of the Pathogenesis-related Protein Superfamily

Milne

Abbenante

Tyndall

et al. 2003

Journal of Biological Chemistry

207

205

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The pathogenesis-related (PR) protein superfamily is widely distributed in the animal, plant, and fungal kingdoms and is implicated in human brain tumor growth and plant pathogenesis. The precise biological activity of PR proteins, however, has remained elusive. Here we report the characterization, cloning and structural homology modeling of Tex31 from the venom duct of Conus textile. Tex31 was isolated to >95% purity by activityguided fractionation using a para-nitroanilide substrate based on the putative cleavage site residues found in the propeptide precursor of conotoxin TxVIA. Tex31 requires four residues including a leucine N-terminal of the cleavage site for efficient substrate processing. The sequence of Tex31 was determined using two degenerate PCR primers designed from N-terminal and tryptic digest Edman sequences. A BLAST search revealed that Tex31 was a member of the PR protein superfamily and most closely related to the CRISP family of mammalian proteins that have a cysteine-rich C-terminal tail. A homology model constructed from two PR proteins revealed that the likely catalytic residues in Tex31 fall within a structurally conserved domain found in PR proteins. Thus, it is possible that other PR proteins may also be substrate-specific proteases.Of the genomes that have been completely sequenced, as many as 2% of the gene products encode known proteases, many of which regulate physiological processes such as blood coagulation, fibrinolysis, the complement system, and the processing of protein hormone precursors by specific convertases. Prohormones and neuropeptides (3-40 amino acids), important coordinators of cellular function in the endocrine and nervous systems, are often synthesized as propeptides. The propeptide is subsequently processed by substrate-specific proteases to yield the mature bioactive form (1). As many of the substratespecific proteases remain unidentified, predicting new bioactive peptides from cDNA sequences is presently difficult, if not impossible (2, 3). Linderström-Lang coined the term "limited proteolysis" to describe enzymes with restricted specificity (4). Enzyme activity can be restricted by substrate structure, enzyme processing state, endogenous protease inhibitor levels or a combination of these factors (5). Peptides derived from prohormones are typically flanked by a pair of dibasic residues (Lys-Arg, Arg-Arg, Lys-Lys, or Arg-Lys) and are cleaved by proteases found in secretory vesicles (1). However, many precursor peptides contain multiple sets of basic residues, suggesting that highly substrate specific or differentially expressed proteases can determine processing outcomes.The venom of cone snails (predatory marine molluscs of the genus Conus) has yielded a rich source of novel neuroactive peptides ("conotoxins") (6). However, the enzymes responsible for cleaving the conotoxins from their propeptide precursors have not been isolated. Here we report the purification, cloning, and initial characterization of Tex31, a protease from venom Conus textile. Interestingly,...

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“…Within fruitbodies the hymenium with basidia is formed in which karyogamy and meiosis occur [110]. Certain fruitbody specific genes have been identified and analyzed, among them the genes Sc7 and Sc14 encoding small hydrophilic proteins with extracellular localization and hydrophobins like Sol and Sc4 [111][112][113][114][115][116][117][118][119][120][121][122][123]. Fruitbody formation and sporulation also can be induced or enhanced by certain factors supplied with the media, e.g.…”

Section: Four O'pes ~F Mating Interactionsmentioning

confidence: 99%

Tetrapolar fungal mating types: Sexes by the thousands

Kothe

1996

FEMS Microbiology Reviews

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In order to achieve genetic rearrangement in a sexual cycle, eukaryotes go through the processes of meiosis and mating. Different mating types assure that mating is only possible between two genetically diverse individuals. Basidiomycetous fungi display thousands of different mating types that are determined by two genetically unlinked loci. One locus is multiallelic and contains genes for homeodomain transcription factors which are able to form heterodimers. The activation of target genes is dependent on heterodimers formed from the monomeric transcription factor proteins originating from different alleles of this genetic locus. The interactions between the two monomeric transcription factors and the activation of target genes by the heterodimeric proteins make this regulatory system both complex and interesting. The second locus contains a pheromone receptor system: the pheromone receptor is similar to the G protein-linked serpentine receptors in Saccharomyces cereeisiae that activate the pheromone response via a phosphorylation signal transduction cascade in S. cerevisiae. This pheromone perception is a trigger of sexual development and not, as with yeast, itself under cbntrol of mating type genes. Rather it directly senses diversity at the mating type loci. Whereas heterobasidiomycetes display a bi-allelic structure for this locus with recognition between one receptor and the opposite pheromone, homobasidiomycetes contain multiple specificities for pheromone receptors and pheromones.

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The Sc7/Sc14 gene family of Schizophyllum commune codes for extracellular proteins specifically expressed during fruit-body formation

Cited by 60 publications

References 21 publications

The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins

The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins

Isolation and Characterization of a Cone Snail Protease with Homology to CRISP Proteins of the Pathogenesis-related Protein Superfamily

Tetrapolar fungal mating types: Sexes by the thousands

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