Sequence Determination and Molecular Characterization of Gigantin, a Cytotoxic Protein Produced by the MouldAspergillus giganteusIFO 5818

Wirth, Jérémie; Pozo, Álvaro Martı́nez del; Mancheño, José M.; Martı́nez-Ruiz, Antonio; Lacadena, Javier; Oñaderra, Mercedes; Gavilanes, José G.

doi:10.1006/abbi.1997.0175

Cited by 22 publications

(18 citation statements)

References 22 publications

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“…4 Several of these fungal ribotoxins, produced by different Aspergillus spp or related genera, have been described 5,6 (and references therein cited), ␣-sarcin from A. giganteus being the most studied. The sequence identity among these proteins 5,6 is high and involves the residues identified as catalytic, [7][8][9][10] as well as two tryptophan residues. 5,6 This similarity is also observed for the known three-dimensional structure of two of these ribotoxins, ␣-sarcin 11,12 and restrictocin 13 from A. restrictus.…”

Section: Introductionmentioning

confidence: 98%

Assignment of the contribution of the tryptophan residues to the spectroscopic and functional properties of the ribotoxin ?-sarcin

et al. 2000

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Section: Introductionmentioning

confidence: 98%

Assignment of the contribution of the tryptophan residues to the spectroscopic and functional properties of the ribotoxin ?-sarcin

et al. 2000

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“…The absorbance was monitored at 280 nm with a Beckman detector module 166. Integration of the peaks and analysis of the results were accomplished with the Beckman System Gold software (44).…”

Section: Methodsmentioning

confidence: 99%

Structure-Activity Relationship of α Mating Pheromone from the Fungal Pathogen Fusarium oxysporum

Vitale

Partida-Hanon

Serrano

et al. 2017

Journal of Biological Chemistry

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Edited by Norma AllewellDuring sexual development ascomycete fungi produce two types of peptide pheromones termed a and ␣. The ␣ pheromone from the budding yeast Saccharomyces cerevisiae, a 13-residue peptide that elicits cell cycle arrest and chemotropic growth, has served as paradigm for the interaction of small peptides with their cognate G protein-coupled receptors. However, no structural information is currently available for ␣ pheromones from filamentous ascomycetes, which are significantly shorter and share almost no sequence similarity with the S. cerevisiae homolog. High resolution structure of synthetic ␣-pheromone from the plant pathogenic ascomycete Fusarium oxysporum revealed the presence of a central ␤-turn resembling that of its yeast counterpart. Disruption of the-fold by D-alanine substitution of the conserved central Gly 6 -Gln 7 residues or by random sequence scrambling demonstrated a crucial role for this structural determinant in chemoattractant activity. Unexpectedly, the growth inhibitory effect of F. oxysporum ␣-pheromone was independent of the cognate G protein-coupled receptors Ste2 and of the central ␤-turn but instead required two conserved Trp 1 -Cys 2 residues at the N terminus. These results indicate that, despite their reduced size, fungal ␣-pheromones contain discrete functional regions with a defined secondary structure that regulate diverse biological processes such as polarity reorientation and cell division.

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“…-Sarcin, restrictocin, and Aspf1 are the most exhaustively characterized ribotoxins (Arruda et al, 1992;García-Ortega et al, 2005;Gasset et al, 1994;Kao et al, 2001;Martínez-Ruiz et al, 2001;Wool, 1997), but many others have been identified and partially characterized within different fungal species (Huang et al,1997;Lin et al, 1995;Martínez-Ruiz et al, 1999a, 1999bParente et al, 1996;Varga and Samson, 2008;Wirth et al, 1997). These studies have shown a high degree of conservation among ribotoxins, as most of those so far characterized display amino acid sequence similarities above 85% (Lacadena et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Fungal extracellular ribotoxins as insecticidal agents

Olombrada¹,

Herrero-Galán²,

Tello³

et al. 2013

Insect Biochemistry and Molecular Biology

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Fungal ribotoxins were discovered almost 50 years ago as extracellular ribonucleases (RNases) with antitumoral properties. However, the biological function of these toxic proteins has remained elusive. The discovery of the ribotoxin HtA, produced by the invertebrates pathogen H. thompsonii, revived the old proposal that insecticidal activity would be their long searched function. Unfortunately, HtA is rather singular among all ribotoxins known in terms of sequence and structure similarities. Thus, it was intriguing to answer the question of whether HtA is just an exception or, on the contrary, the paradigmatic example of the ribotoxins function. The work presented uses HtA and -sarcin, the most representative member of the ribotoxins family, to show their strong toxic action against insect larvae and cells.

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Sequence Determination and Molecular Characterization of Gigantin, a Cytotoxic Protein Produced by the MouldAspergillus giganteusIFO 5818

Cited by 22 publications

References 22 publications

Assignment of the contribution of the tryptophan residues to the spectroscopic and functional properties of the ribotoxin ?-sarcin

Assignment of the contribution of the tryptophan residues to the spectroscopic and functional properties of the ribotoxin ?-sarcin

Structure-Activity Relationship of α Mating Pheromone from the Fungal Pathogen Fusarium oxysporum

Fungal extracellular ribotoxins as insecticidal agents

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