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proteinase inhibitor/pomme de terre
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Structure and folding of potato type II proteinase inhibitors: circular permutation and intramolecular domain swapping.
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Potato type II serine proteinase inhibitors are proteins that consist of multiple sequence repeats, and exhibit a multidomain structure. The structural domains are circular permutations of the repeat sequence, as a result of intramolecular domain swapping. Structural studies give indications for the
Antisense-mediated depletion of a potato lipoxygenase reduces wound induction of proteinase inhibitors and increases weight gain of insect pests.
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De novo jasmonic acid (JA) synthesis is required for wound-induced expression of proteinase inhibitors and other defense genes in potato and tomato. The first step in JA biosynthesis involves lipoxygenase (LOX) introducing molecular oxygen at the C-13 position of linolenic acid. We previously have
Wound-inducible nuclear protein binds DNA fragments that regulate a proteinase inhibitor II gene from potato.
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Deletion analysis from the 3' to the 5' end of the promoter region of the wound-inducible potato proteinase inhibitor IIK gene has identified a 421-base sequence at -136 to -557 that is necessary for expression. Utilizing DNA band-shift assays, a 10-base sequence within the 421-base region was found
Identification of potato nuclear proteins binding to the distal promoter region of the proteinase inhibitor II gene.
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Potato nuclear proteins specifically bind to a DNA sequence at the most 5' distal region of the promoter of a potato proteinase inhibitor II gene. Binding studies using the electrophoretic mobility-shift assay showed the appearance of two protein-DNA complexes in the presence of both tuber and leaf
Inhibition of Colorado potato beetle larvae by a locust proteinase inhibitor peptide expressed in potato.
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The cDNA for a 73-mer peptide containing two locust serine proteinase inhibitors was cloned, fused to the constitutive CaMV35S promoter and introduced into potato by Agrobacterium-mediated transformation. From 23 independent transgenic lines, three with high mRNA level and proteinase inhibitory
Amino acid sequence of an active fragment of potato proteinase inhibitor IIa.
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The complete amino acid sequence of an active fragment of potato proteinase inhibitor IIa has been established by the Edman degradation procedure and the carboxypeptidase technique. Sequence analyses were carried out on the reduced and carboxymethylated active fragment and its tryptic peptides. To
Isolation of a low molecular weight active fragment of potato proteinase inhibitor IIb.
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A low molecular weight active fragment of potato proteinase inhibitor IIPB was obtained by incubating the inhibitor with an equimolar amount of trypsin [EC 3.4.21.4] at pH 8 and 30 degrees for 16 hr, followed by gel filtration through Sephadex G-50, treatment with trichloroacetic acid, and
Selective loss of cysteine residues and disulphide bonds in a potato proteinase inhibitor II family.
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Disulphide bonds between cysteine residues in proteins play a key role in protein folding, stability, and function. Loss of a disulphide bond is often associated with functional differentiation of the protein. The evolution of disulphide bonds is still actively debated; analysis of naturally
Functional analysis of the 3' control region of the potato wound-inducible proteinase inhibitor II gene.
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Proteinase inhibitor genes are expressed strongly in specific plant tissues under both developmental and environmental regulation. We have studied the role of the 3' control region of the potato proteinase inhibitor II gene (PI-II) that is inducible in leaves in response to herbivore attacks or
Potato type I and II proteinase inhibitors: modulating plant physiology and host resistance.
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Serine protease inhibitors (PIs) are a large and complex group of plant proteins. Members of the potato type I (Pin1) and II (Pin2) proteinase inhibitor families are among the first and most extensively characterized plant PIs. Many insects and phytopathogenic microorganisms use intracellular and
A leaf-specific 27 kDa protein of potato Kunitz-type proteinase inhibitor is induced in response to abscisic acid, ethylene, methyl jasmonate, and water deficit.
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The 22 kDa Kunitz-type potato proteinase inhibitor (22 kDa KPPI) was induced in tubers. However, the 27 kDa protein, which is immunologically related to the 22 kDa KPPI, was induced in leaves by wounding, hormones, and environmental stresses. The leaf-specific 27 kDa protein was induced in leaves
[Inhibition of cathepsins from trout muscle and from bovine spleen by proteinase inhibitors of potato tubers (author's transl)].
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The cathepsins D from trout muscle and from bovine spleen, as well as cathepsin A from bovine spleen are inhibited by a crude proteinase inhibitor from potato tubers. Cathepsins C and B1 are not inhibited. It was shown by isoelectric focussing that several inhibitors for cathepsin D are present in
Amino acid sequence of an active fragment of potato proteinase inhibitor IIb.
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The amino acid sequence of an active fragment of potato proteinase inhibitor IIb was determined by the Edman degradation procedure and the carboxypeptidase technique. Analyses were carried out on peptides derived from the reduced and carboxymethylated active fragment by digestion with trypsin and
Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2.
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An automated method, based on the principle of simulated annealing, is presented for determining the three-dimensional structures of proteins on the basis of short (less than 5 A) interproton distance data derived from nuclear Overhauser enhancement (NOE) measurements. The method makes use of
Colorado potato beetle larvae on potato plants expressing a locust proteinase inhibitor.
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The natural defence system of plants often involves inhibitors of digestive enzymes of their pests. Modem and environmental-friendly methods try to increase this plant resistance by expressing heterologous protease inhibitors in crops. Here we report the effects of expressing a gene from desert
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