Characterization and Analysis of Thionin Genes

Garcı́a-Olmedo, Francisco; Carmona, Marı́a José; López-Fando, Juan; Fernández, J. A.; Castagnaro, Atilio Pedro; Molina, Antonio; Hernández-Lucas, C.; Carbonero, Pilar

doi:10.1007/978-3-7091-6684-0_11

Cited by 52 publications

(52 citation statements)

References 41 publications

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“…The sequence has none of the highlyconserved features of Bowman-Birk inhibitors [2], while it is clearly homologous to a family of proteins, of which the first one to be reported was designated y-thionin [5, 61. This was an inadequate name because a-thionin and P-thionin are two closely related variants of just one of the five types of thionins described [4], and the so-called y-thionin was not homologous to any of them, although it is also basic, cysteine rich and of similar size. The separation from Bowman-Birk inhibitors and from true thionins is further justified because Pth-Stl did not inhibit trypsin, even at much higher concentrations than those required for true Bowman-Birk inhibitors, and had little or no effect on cell-free protein synthesis or on P-glucuronidase, at concentrations that are inhibitory in the case of true thionins.…”

Section: Discussionmentioning

confidence: 99%

Pseudothionin‐St1, a potato peptide active against potato pathogens

Moreno¹,

Segura²,

Garcı́a-Olmedo³

1994

European Journal of Biochemistry

124

101

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A 5‐kDa polypeptide, pseudothionin Solanum tuberosum 1(Pth‐St1), which was active against Clavibacter michiganensis subspecies sepedonicus, a bacterial pathogen of potatoes, has been purified from the buffer‐insoluble fraction of potato tubers by salt extraction and HPCL. Pth‐St1 was also active against other potato pathogens tested (Pseudomonas solanacearum and Fusarium solani). The N‐terminal amino acid sequence of this peptide was identical (except for a N/H substitution at position 2) to that deduced from a previously reported cDNA sequence (EMBL accession number X‐13180), which had been misclassified as a Bowman‐Birk protease inhibitor. Pth‐St1 did not inhibit either trypsin or insect α‐amylase activities, and, in contrast with true thionins, did not affect cell‐free protein synthesis or β‐glucuronidase activity. Northern‐blot and tissue‐print analyses showed that steady‐state mRNA levels were highest in flowers (especially in petals), followed by tubers (especially in the epidermal cell layers and in leaf primordia), stems and leaves. Infection of leaves with a bacterial pathogen suspended in 10 mM MgCl2 switched off the gene, whereas mock inoculation with 10 mM MgCl2 alone induced higher mRNA levels.

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Section: Discussionmentioning

confidence: 99%

Pseudothionin‐St1, a potato peptide active against potato pathogens

Moreno¹,

Segura²,

Garcı́a-Olmedo³

1994

European Journal of Biochemistry

124

101

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“…There are one or two genes of type I per haploid genome in group-1 chromosomes of wheat and barley genomes. These genes encode precursor proteins in which the sequence of the mature protein is preceded by that of a signal peptide that is co-translationally processed and followed by that of a C-terminal, acidic peptide that undergoes a posttranslational excisión (Ponz et al 1983;García-Olmedo et al 1992) .…”

Section: Thioninsmentioning

confidence: 99%

Expression of Genes Encoding Thionins and Lipid-Transfer Proteins. A Combinatorial Model for the Responses of Defense Genes to Pathogens.

Molina¹,

Garcı́a-Olmedo²

1994

Plant Molecular Biology

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“…Thionins, which were the first plant peptides for which an antipathogenic activity had been reported [3,4], have been shown to alter cell membrane permeability [5,6] and to interact with artificial liposomes containing phosphatidylserine [7,8]. Wheat a-thionin contains 45 amino acid residues, with a charge/mass ratio of +2X1CT 3 [4].…”

Section: Introductionmentioning

confidence: 99%

“…Wheat a-thionin contains 45 amino acid residues, with a charge/mass ratio of +2X1CT 3 [4]. Plant defensins, which are phylogenetically separate but structurally similar to thionins, do not seem to cause substantial membrane permeabilization [6].…”

Section: Introductionmentioning

confidence: 99%

Differential effects of five types of antipathogenic plant peptides on model membranes

Caaveiro

Molina²,

González-Mañas

et al. 1997

FEBS Letters

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The effects of five antipathogenic plant peptides, wheat a-thionin, potato PTH1 defensin, barley LTP2 lipid transfer protein, and potato tuber DL1 and DL2 defensins, have been tested against phospholipid vesicles (liposomes). Wheat thionin very actively induces aggregation and leakage of negatively charged vesicles. LTP2 displays the same activities, although to a limited extent. Under certain conditions PTH1 and DL2 induce vesicle aggregation, but not leakage. Potato defensin DL1 failed to show any effect on liposomes. The same peptides have been assayed against a plant pathogenic bacterium, both the membrane-active and -inactive compounds having efficient antibacterial action.

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Characterization and Analysis of Thionin Genes

Cited by 52 publications

References 41 publications

Pseudothionin‐St1, a potato peptide active against potato pathogens

Pseudothionin‐St1, a potato peptide active against potato pathogens

Expression of Genes Encoding Thionins and Lipid-Transfer Proteins. A Combinatorial Model for the Responses of Defense Genes to Pathogens.

Differential effects of five types of antipathogenic plant peptides on model membranes

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