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Volumn 10, Issue 1, 1998, Pages 16-22

Antimicrobial proteins in induced plant defense

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; VEGETABLE PROTEIN;

EID: 0032006219     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(98)80025-3     Document Type: Article
Times cited : (192)

References (65)
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    • of outstanding interest. A major breakthrough in the search for molecular events downstream of avr - R recognition. Using the two-hybrid system, the authors identified plant genes encoding Pto-interacting (Pti) proteins. Pti4/5/6 have features of transcription factors and bind to ethylene-responsive cis-elements on promoters of genes for basic PR proteins. The data provide unexpected and striking evidence for a direct functional link between an R gene product and defense gene expression.
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    • Polypeptide signaling for plant defensive genes exhibits analogies to defense signaling in animals
    • of special interest. This paper highlights some functional similarities between the tomato defense signaling pathway activated by insect attacks and defense signaling in animal macrophages. Both systems use polypeptide- and lipid-based strategies to activate defense responses.
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    • NMR solution of the pathogenesis-related protein P14a
    • of special interest. The three-dimensional structure of PR-1 and PR-5 proteins provides initial clues for identification of the active sites and the mode of action of these antimicrobial proteins. See also [43].
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    • The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family
    • of special interest. The three-dimensional structure of PR-1 and PR-5 proteins provides initial clues for identification of the active sites and the mode of action of these antimicrobial proteins. See also [42].
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    • Stress proteins on the yeast cell surface determine resistance to osmotin, a plant antifungal protein
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