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The potato sucrose transporter StSUT1 interacts with a DRM-associated protein disulfide isomerase.

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Organization of proteins into complexes is crucial for many cellular functions. Recently, the SUT1 protein was shown to form homodimeric complexes, to be associated with lipid raft-like microdomains in yeast as well as in plants and to undergo endocytosis in response to brefeldin A. We therefore

Effect of N-nitrosoamines and nitrosationable pesticide tetramethylthiuram disulfide on soil microbiocenosis and potato yield: a model system.

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The effect of carcinogenic N-nitrosoamines (NA), NA-producing tetramethylthiuram disulfide (TMTD) pesticide, and of various doses of nitrogen fertilizers (90, 180, and 270 kg/ha) on the forming and vital functions of microbiocenosis of light gray forest soil was studied. The quantity, nitrifying

Structures of scrambled disulfide forms of the potato carboxypeptidase inhibitor predicted by molecular dynamics simulations with constraints.

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The structures of two species of potato carboxypeptidase inhibitor with nonnative disulfide bonds were determined by molecular dynamics simulations in explicit solvent using disulfide bond constraints that have been shown to work for the native species. Ten structures were determined; five for

Refolding of potato carboxypeptidase inhibitor by molecular dynamics simulations with disulfide bond constraints.

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The folding of the potato carboxypeptidase inhibitor (PCI) from partially unfolded conformations by the introduction of native disulfide bond constraints was studied by molecular dynamics simulations in explicit solvent. PCI consists of a globular core (Cys8 to Cys34), two flexible terminal regions

The disulfide folding pathway of potato carboxypeptidase inhibitor.

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Potato carboxypeptidase inhibitor (PCI) contains 39 amino acids and three disulfides. Reduced and denatured PCI refolds spontaneously in vitro to regain its native structure. The folding pathway of a recombinant form of this protein has been elucidated by structural analysis and stop/go folding

Reduction and carboxamidomethylation of the single disulfide bond of proteinase inhibitor I from potato tubers. Effects on stability, immunological properties, and inhibitory activities.

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The single disulfide bond in potato Inhibitor I protomers (Mr = 8,000) was reduced and alkylated in the absence of denaturants to the carboxamidomethyl cysteine derivative. Two half-cystines per mol of inhibitor protomer were modified as determined by (a) loss of two sulfhydryl groups per reduced

The role of disulfide bonds in a Solanum tuberosum saposin-like protein investigated using molecular dynamics

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The Solanum tuberosum plant specific insert (StPSI) has a defensive role in potato plants, with the requirements of acidic pH and anionic lipids. The StPSI contains a set of three highly conserved disulfide bonds that bridge the protein's helical domains. Removal of these bonds leads to enhanced

Selective removal of individual disulfide bonds within a potato type II serine proteinase inhibitor from Nicotiana alata reveals differential stabilization of the reactive-site loop.

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The 53-amino-acid trypsin inhibitor 1 from Nicotiana alata (T1) belongs to the potato type II family also known as the PinII family of proteinase inhibitors, one of the major families of canonical proteinase inhibitors. T1 contains four disulfide bonds, two of which (C4-C41 and C8-C37) stabilize the

Structure of potato carboxypeptidase inhibitor: disulfide pairing and exposure of aromatic residues.

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The determination of the covalent structure of a carboxypeptidase inhibitor from potatoes containing 39 amino acid residues has been completed by analysis of the pairing of the six half-cystine residues. Since the native inhibitor is resistant to fragmentation by proteases, the protein was first

Fluorescence studies with potato carboxypeptidase inhibitor.

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Potato carboxypeptidase inhibitor (CPI) is a 39-residue globular protein whose X-ray structure is known. The protein's two tryptophan residues (W22 and W28) appear to be on the surface in the crystal structure. The fluorescence spectrum of CPI has a maximum at 344 nm. Acrylamide solute quenching

Expression of a synthetic gene encoding potato carboxypeptidase inhibitor using a bacterial secretion vector.

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A synthetic gene encoding the 39-amino-acid (aa) potato carboxypeptidase inhibitor IIa (PCI-IIa) has been constructed and expressed using the secretion vector, pIN-III-ompA-3, fused in frame to the OmpA signal peptide-encoding sequence. Recombinant Escherichia coli secreted a PCI with 10 additional

LTCI, a novel chymotrypsin inhibitor of the potato I family from the earthworm Lumbricus terrestris. Purification, cDNA cloning, and expression.

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A novel chymotrypsin inhibitor of the potato I protease inhibitor family from the earthworm Lumbricus terrestris was purified. The inhibitor, named LTCI, was isolated by methanol extraction, affinity chromatography on immobilized methylchymotrypsin, and ion exchange chromatography followed by

Cloning and sequencing of a cDNA encoding acetylcholinesterase in Colorado potato beetle, Leptinotarsa decemlineata (Say).

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A cDNA encoding acetylcholinesterase (AChE, EC 1.1.1.7) was cloned from a cDNA library constructed from an insecticide-susceptible strain of Colorado potato beetle, Leptinotarsa decemlineata (Say). The complete amino acid sequence of AChE deduced from the cDNA consisted of 29 residues for the

Inhibition of phytoalexin synthesis in arachidonic Acid-stressed potato tissue by inhibitors of lipoxygenase and cyanide-resistant respiration.

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Arachidonic acid-stressed potato tuber discs synthesized the phytoalexin rishitin. This synthesis was inhibited by salicylhydroxamic acid (SHAM), and to a lesser extent by tetraethylthiuram disulfide (disulfiram). Disulfiram was less effective apparently because it was inactivated in the tuber

Volatile compounds from potato-like model systems.

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The volatile reaction products of aqueous mixtures comprising combinations of methionine, glucose, linoleic acid, and starch heated in a modified Likens-Nickerson apparatus were extracted and analyzed by gas chromatography-mass spectrometry (GC-MS). The majority of volatile compounds were formed

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