phaseolin/phaseolus

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In vivo endoproteolytically cleaved phaseolin is stable and accumulates in developing Phaseolus lunatus L. seeds.

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Phaseolin is the most abundant storage protein of bean seeds. To modify its amino-acidic composition by protein engineering, for the improvement of its nutritional value, regions which could be modified without detrimental effects on structural features of the protein must be identified. Data

Detection of rRNA and phaseolin genes on polytene chromosomes of Phaseolus coccineus by fluorescence in situ hybridization after pepsin pretreatment.

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This is the first report of fluorescence in situ hybridization (FISH) on plant polytene chromosomes. Different protease pretreatments have been tested to improve fluorescence in situ hybridization FISH on polytene chromosomes of a plant, Phaseolus coccineus, with the aim to enable the detection of

Phaseolin seed variability in common bean (Phaseolus vulgaris L.) by capillary gel electrophoresis.

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Phaseolin, the major seed storage protein of Phaseolus vulgaris from forty-four wild and cultivated accessions, was studied using sodium dodecyl sulphate-capillary gel electrophoresis (SDS-CGE). In total, eleven phaseolin profiles, revealing polypeptide subunit variation in the range from 45.6 kDa

Susceptibility of phaseolin (Phaseolus vulgaris) subunits to trypsinolysis and influence of dietary level of raw phaseolin on protein digestion in the small intestine of rats.

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The aim of the present work was (a) to investigate trypsinolysis of denatured purified T phaseolin (Phaseolus vulgaris) subunits by MS and (b) to test the effect of raw T phaseolin inclusion level in diets fed chronically to rats on digestion in the small intestine. The diets contained casein as the

An engineered C-terminal disulfide bond can partially replace the phaseolin vacuolar sorting signal.

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Seed storage proteins accumulate either in the endoplasmic reticulum (ER) or in vacuoles, and it would appear that polymerization events play a fundamental role in regulating the choice between the two destinies of these proteins. We previously showed that a fusion between the Phaseolus vulgaris

PvAlf, an embryo-specific acidic transcriptional activator enhances gene expression from phaseolin and phytohemagglutinin promoters.

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Mutations in Vp1 and ABl3 genes of maize and Arabidopsis lead to drastic reductions in the synthesis of a subset of maturation-specific products including seed storage proteins. Gene Phaseolus vulgaris ABl3-like factor (PvAlf), whose protein product is similar to the ABl3 and Vp1 proteins, has been

Immunocytochemical localization of the storage protein phaseolin in the embryo-suspensor of Phaseolus coccineus.

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Antibodies against the bean storage protein, phaseolin, were induced in rabbits. Sections of bean embryos of various age were incubated with the antibodies, and exposed to fluorescein isocyanate (FITC) conjugated goat anti-rabbit immunoglobulin. Distinct positive signals were found in vacuoles of

Lima bean (Phaseolus lunatus) seed coat phaseolin is detrimental to the cowpea weevil (Callosobruchus maculatus).

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The presence of phaseolin (a vicilin-like 7S storage globulin) peptides in the seed coat of the legume Phaseolus lunatus L. (lima bean) was demonstrated by N-terminal amino acid sequencing. Utilizing an artificial seed system assay we showed that phaseolin, isolated from both cotyledon and testa

Analyzing bean extracts using time-dependent SDS trapping to quantify the kinetic stability of phaseolin proteins.

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In common beans and lima bean, the storage protein phaseolin is difficult to degrade and SDS-resistant, a sign of kinetic stability. Kinetically stable proteins (KSPs) are characterized by having a high-energy barrier between the native and denatured states that results in very slow unfolding. Such

Crosslinking of microsomal proteins identifies P-9000, a protein that is co-transported with phaseolin and phytohemagglutinin in bean cotyledons.

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Developing cotyledons of the common bean, Phaseolus vulgaris L., transport within their secretory system (endoplasmic reticulum and Golgi apparatus) the abundant vacuolar proteins, phaseolin and phytohemagglutinin. To identify proteins that may play a role in vacuolar targeting, we treated cotyledon

Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins.

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The refinement to 2.2 A resolution of the three-dimensional structure of the seed storage protein phaseolin from the French bean (Phaseolus vulgaris) via an alternative crystal form is described. The refined structure reveals details of the molecule hitherto unobserved and in particular we identify

Cell Ablation Reveals That Expression from the Phaseolin Promoter Is Confined to Embryogenesis and Microsporogenesis.

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Most previous studies of the [beta]-phaseolin (phas) gene, which encodes the major storage protein in bean (Phaseolus vulgaris L.), have shown its expression to be rigorously confined to the developing seed, both in bean and transgenic tobacco (Nicotiana tabacum L. cv Xanthi) plants. To confirm

Does an asparaginyl-specific cysteine endopeptidase trigger phaseolin degradation in cotyledons of kidney bean seedlings?

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An asparaginyl-specific cysteine endopeptidase which was named 'legumain-like proteinase' (LLP) and has an apparent molecular mass of 38.1 kDa was isolated from cotyledons of kidney bean (Phaseolus vulgaris L.) seedlings and partially characterized. It is, to our knowledge, the first known

Evaluating two-dimensional electrophoresis profiles of the protein phaseolin as markers of genetic differentiation and seed protein quality in common bean (Phaseolus vulgaris L.).

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High-resolution two-dimensional electrophoresis (2-DE) profiles of the protein phaseolin, the major seed storage protein of common bean, display great number of spots with differentially glycosylated and phosphorylated α- and β-type polypeptides. This work aims to test whether these complex profiles

Analysis of common bean expressed sequence tags identifies sulfur metabolic pathways active in seed and sulfur-rich proteins highly expressed in the absence of phaseolin and major lectins.

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BACKGROUND A deficiency in phaseolin and phytohemagglutinin is associated with a near doubling of sulfur amino acid content in genetically related lines of common bean (Phaseolus vulgaris), particularly cysteine, elevated by 70%, and methionine, elevated by 10%. This mostly takes place at the

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