Endopolygalacturonases
Mostrando 1-8 de 8 artigos, teses e dissertações.
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1. Caracterização da expressão de inibidores de poligalacturonases (PGIPs) em resposta aos estresses biótico e abiótico em plantas de feijão comum (Phaseolus vulgaris L.) / Characterization of the expression of polygalacturonase inhibitors (PGIPs) in response to biotic and abiotic stresses in plants of common bean (Phaseolus vulgaris L.)
Sclerotinia sclerotiorum (Lib.) de Bary is a necrotrophic fungal pathogen that causes the disease known as white mold in many plants. During infection, it secretes several endopolygalacturonases (PGs) to degrade cell wall pectin. To counteract the action of PGs, plants express polygalacturonases-inhibiting proteins (PGIPs) that reduce the hydrolytic activity
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 26/11/2011
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2. Caracterização da expressão de inibidores de poligalacturonases (PGIPs) em resposta aos estresses biótico e abiótico em plantas de feijão comum (Phaseolus vulgaris L.) / Characterization of the expression of polygalacturonase inhibitors (PGIPs) in response to biotic and abiotic stresses in plants of common bean (Phaseolus vulgaris L.)
Sclerotinia sclerotiorum (Lib.) de Bary é um fungo necrotrófico patogênico causador da doença conhecida como mofo branco em muitas plantas. Durante a infecção, secreta várias endopoligalacturonases (endo-PGs) que degradam a pectina da parede celular da planta hospedeira. Para contrapor à ação das PGs, as plantas produzem proteínas inibidoras de po
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 26/11/2011
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3. Characterization of the dry bean polygalacturonase-inhibiting protein (PGIP) gene family during Sclerotinia sclerotiorum (Sclerotiniaceae) infection.
Polygalacturonase-inhibiting proteins are leucine-rich repeat proteins that inhibit fungal endopolygalacturonases. The interaction of polygalacturonase-inhibiting protein with endopolygalacturonases limits the destructive potential of endopolygalacturonases and may trigger plant defense responses induced by oligogalacturonides. We examined the expression of
Genetics and Molecular Research. Publicado em: 2011
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4. Host-Pathogen Interactions: VI. A Single Plant Protein Efficiently Inhibits Endopolygalacturonases Secreted by Colletotrichum Lindemuthianum and Aspergillus Niger1
Endopolygalacturonases have been purified from the extracellular enzymes of Colletotrichum lindemuthianum and Aspergillus niger. A protein, purified from Red Kidney (Phaseolus vulgaris) beans for its ability to inhibit the endopolygalacturonase secreted by C. lindemuthianum, inhibits the A. niger endopolygalacturonase almost as efficiently as it inhibits the
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5. Proteinase inhibitor-inducing factor activity in tomato leaves resides in oligosaccharides enzymically released from cell walls
The synthesis and accumulation of proteinase inhibitor I in excised tomato leaves can be induced with oligosaccharides obtained by fungal endo-α-1,4-polygalacturonase digestion of a pectic polysaccharide (Mr 5000-10,000) isolated from tomato leaves. Active oligosaccharides were also released from isolated tomato leaf cell walls by endopolygalacturonases par
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6. The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense
Polygalacturonase-inhibiting proteins (PGIPs) are plant cell wall proteins that protect plants from fungal invasion. They interact with endopolygalacturonases secreted by phytopathogenic fungi, inhibit their enzymatic activity, and favor the accumulation of oligogalacturonides, which activate plant defense responses. PGIPs are members of the leucine-rich
National Academy of Sciences.
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7. Common amino acid domain among endopolygalacturonases of ascomycete fungi.
The endopolygalacturonase (EC 3.2.1.15) enzymes produced in vitro by three ascomycete fungi, Aspergillus niger, Sclerotinia sclerotiorum, and Colletotrichum lindemuthianum were studied by using thin-layer isoelectric focusing and activity stain overlay techniques. The polygalacturonases from A. niger and S. sclerotiorum consisted of numerous isoforms, wherea
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8. Characterization of the Complex Locus of Bean Encoding Polygalacturonase-Inhibiting Proteins Reveals Subfunctionalization for Defense against Fungi and Insects1
Polygalacturonase-inhibiting proteins (PGIPs) are extracellular plant inhibitors of fungal endopolygalacturonases (PGs) that belong to the superfamily of Leu-rich repeat proteins. We have characterized the full complement of pgip genes in the bean (Phaseolus vulgaris) genotype BAT93. This comprises four clustered members that span a 50-kb region and, based o
American Society of Plant Biologists.