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PubMed1982

Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli.

The structural gene of the sweet-tasting plant protein (prepro)thaumatin was cloned and expressed in Escherichia coli. Expression was effected under control of lac and trp promoter/operator systems and through the use of bacterial ribosome-binding sites. The naturally occurring thaumatin II represents a processed form. The primary translation product, preprothaumatin, of the cloned mRNA-derived cDNA contains extensions at both the amino terminus and the carboxy terminus. The amino terminal extension of 22 amino acids is hydrophobic and very much resembles an excretion-related signal sequence. The six amino acids-long carboxy terminal extension is very acidic in character, in contrast to the overall highly basic thaumatin molecule. The possible role of such an acidic tail with respect to compartmentalization is discussed.

Base Sequence↗
PubMed2007

Phosphorylation studies using plant protein microarrays.

Identifying protein kinase substrates is one major focus of protein kinase research and supports the elucidation of signal transduction pathways and their complex regulation. In this chapter we describe a protein microarray-based in vitro method, which permits a systematic screening of immobilized proteins for their phosphorylation by specific protein kinases. This high-throughput method allows the identification of potential kinase substrates. The method starts with plant protein microarrays containing hundreds of purified recombinant His-tagged proteins. The microarrays have to be incubated with the soluble and active kinase in the presence of radioactive [gamma33-P]ATP. Only small volumes of active kinase are needed for one microarray experiment. Radioactive signals are then detectable by phosphor imager or X-ray film. The identified potential substrates have to be verified by other in vitro or in vivo methods, as both the kinase and the substrate may not interact with each other under in vivo conditions. This screening method could be generally applicable for direct identification of candidate substrates of various protein kinases.

Arabidopsis↗
PubMed2004

A cysteine-rich plant protein potentiates Potyvirus movement through an interaction with the virus genome-linked protein VPg.

We have identified a cellular factor that interacts with the virus genome-linked proteins (VPgs) of a diverse range of potyviruses. The factor, called Potyvirus VPg-interacting protein (PVIP), is a plant-specific protein with homologues in all the species examined, i.e., pea, Arabidopsis thaliana, and Nicotiana benthamiana. The sequence of PVIP does not identify a specific function, although the existence of a "PHD finger" domain may implicate the protein in transcriptional control through chromatin remodeling. Deletion analysis using the yeast two-hybrid system showed that the determinants of the interaction lay close to the N terminus of VPg; indeed, the N-terminal 16 amino acids were shown to be both necessary and sufficient for the interaction with at least one PVIP protein. From a sequence comparison of different potyvirus VPg proteins, a specific amino acid at position 12 was directly implicated in the interaction. This part of VPg is distinct from regions associated with other functional roles of VPg. Through mutation of Turnip mosaic virus (TuMV) at VPg position 12, we showed that the interaction with PVIP affected systemic symptoms in infected plants. This resulted from reduced cell-to-cell and systemic movement more than reduced virus replication, as visualized by comparing green fluorescent protein-tagged wild-type and mutant viruses. Furthermore, by using RNA interference of PVIP in Arabidopsis, we showed that reduced expression of PVIP genes reduced susceptibility to TuMV infection. We conclude that PVIP functions as an ancillary factor to support potyvirus movement in plants.

Amino Acid Motifs↗
PubMed1989

Transplantation of skin grafts in rats fed plant protein wheat gluten.

The effects of diets containing low biologic value plant protein wheat gluten and the high biologic value protein casein on skin allograft survival were studied in growing Charles River (C.D. strain) rats. Five groups of weanling rats were fed 16% casein or gluten with or without supplementation with the amino acids L-lysine and L-threonine. Allografts were obtained from the hooded Lister strain. Autograft experiments were also performed. The skin bed and the allografts were prepared by round-punch biopsies, and the grafts were retained in situ by cellophane tape dressings. In the gluten-fed rats, no rejection of allografts was observed during the 45-day study period. In the casein-fed rats, a 90% rejection rate occurred on Days 10-14 after transplantation. The absence of rejection in gluten-fed rats may be explained by an impaired cellular immune response due to protein malnutrition. Supplementing the gluten diet with the essential amino acids L-lysine and L-threonine restored the rejection rate to that of the control rats. The cell-mediated immune response, as measured by in vitro stimulation of lymphocytes with the mitogen concanavalin A, was severely impaired by the gluten diet. These experiments indicate that low biologic value protein diet in the rat is associated with skin allograft acceptance, probably due to impairment of cell-mediated immunity.

Animals↗
PubMed2026

The domestication-associated WHP10 tandem cluster of amino acid transporter genes enhances whole-plant protein accumulation in maize.

Improving protein accumulation in maize is essential for sustainable agriculture, yet the regulatory mechanisms governing the intermediate "flow" of organic nitrogen remain elusive. Here, we show that the maize stem acts as a regulatory node for nitrogen allocation. By integrating spatial transcriptomics and metabolomics with quantitative genetics, we demonstrate that a transport-oriented stem program orchestrates the high-protein phenotype of the wild maize accession Ames21814. We identified a major locus, Whole-plant High Protein 10 (WHP10), that encodes a tandemly duplicated cluster of amino acid transporter genes. WHP10 exhibits strong vascular-biased expression, driven by promoter divergence that enhances the wild allele's activity. Functional assays and genetic validation support a model in which the WHP10 cluster facilitates the transport of multiple nitrogen-rich amino acids, thereby contributing to vascular-associated amino acid transport and post-uptake organic-nitrogen partitioning. Our findings establish stem flow as a regulatory layer for protein accumulation and identify WHP10 as a high-value target for precision breeding to enhance whole-plant protein accumulation without compromising grain yield.

Zea mays↗
PubMed2006

Expression of the sweet-tasting plant protein brazzein in Escherichia coli and Lactococcus lactis: a path toward sweet lactic acid bacteria.

Brazzein is an intensely sweet-tasting plant protein with good stability, which makes it an attractive alternative to sucrose. A brazzein gene has been designed, synthesized, and expressed in Escherichia coli at 30 degrees C to yield brazzein in a soluble form and in considerable quantity. Antibodies have been produced using brazzein fused to His-tag. Brazzein without the tag was sweet and resembled closely the taste of its native counterpart. The brazzein gene was also expressed in Lactococcus lactis, using a nisin-controlled expression system, to produce sweet-tasting lactic acid bacteria. The low level of expression was detected with anti-brazzein antibodies. Secretion of brazzein into the medium has not led to significant yield increase. Surprisingly, optimizing the codon usage for Lactococcus lactis led to a decrease in the yield of brazzein.

Amino Acid Sequence↗
PubMed2000

Selected animal and plant protein sources affect nutrient digestibility and fecal characteristics of ileally cannulated dogs.

The objective of this study was to compare ileal and total tract nutrient digestibilities and fecal characteristics of dogs fed selected animal and plant protein sources incorporated into grain-based diets. Four crude protein sources--soybean meal (SBM), poultry meal (PM), poultry by-product meal (PBPM), and beef and bone meal (BBM)--were fed to four ileal cannulated dogs in a 4 x 4 Latin square design. Intakes of dry matter, organic matter, crude protein, and fat by dogs were similar. Total dietary fiber (TDF) intake was highest for the SBM treatment compared to other treatments. Ileal digestibilities of DM, OM, CP, fat, and TDF were not affected by treatment. Total tract digestibility of DM was lower for the BBM and SBM diets, while OM digestibility was lower for the SBM treatment only. Total tract CP digestibility was similar for BBM, PBPM, and SBM treatments and was higher for the PM treatment. As-is fecal excretion [g/d] was greater when dogs received the SBM treatment. Fecal output on a DM basis was higher for the SBM treatment compared to the other treatments. All diets were well utilized by the dogs as assessed by ileal and total tract digestibility data and fecal characteristics.

Amino Acids↗
PubMedDate not supplied

[Effect of plant protein on pancreatic exocrine function in chronic kidney failure patients].

Patients with chronic renal failure received the diet in which plant protein accounted for 80% of protein component. There was a definite decline in the serum of amylase and lipase activity. The activity of trypsin and its inhibitor remained the same whereas the control group manifested its elevation. In administering the diet for a long time one should consider the possibilities of the occurrence of the action of plant proteinase inhibitors.

Adult↗
PubMed2006

Distributional gradient of amino acid repeats in plant proteins.

A computer-based analysis was conducted to assess the characteristics of amino acid repeats in Arabidopsis and rice. Our analysis showed a negative gradient in amino acid repeat distribution along the direction of translation in plants. Repeat occurrences are obviously associated with position in plant proteins but are not consistent with the corresponding amino acid contents. These repeats are encoded by the mixed synonymous codons rather than the uninterrupted reiterations of a single codon, and both Arabidopsis and rice have gradients in their distribution. Functional investigation showed that these repeat-containing proteins are preferentially involved in transcription regulation and protein ubiquitination but significantly underrepresented in the processes of DNA recombination and DNA replication. These data reveal that the direction-related mutation bias and functional selection have influenced the distribution of amino acid repeats in plants.

Arabidopsis↗
PubMed1992

[Directed mutagenesis of genes of some plant proteins].

Mutagenesis of two previously cloned plant genes, maize storage protein cZ22B1 gene and barley Photosystem II protein D1 gene (psbA), was carried out. To improve the nutritional quality of zein, the DNA region corresponding to the protein sixth alpha-helix rod was substituted by a synthetic segment bearing three codon changes for Lys. Additional stabilization of this helix was achieved by three more codon changes for Glu. By means of oligonucleotide directed mutagenesis five different copies of psbA gene were obtained, bearing single codon change of Ser264 (wild type) for Gly, Ala, Cys, Asn, and Thr, respectively. These constructs can be used for studying functional topography of protein D1 and core region.

Amino Acid Sequence↗
PubMed1994

Plant proteins that bind to the 3'-terminal sequences of the negative-strand RNA of three diverse positive-strand RNA plant viruses.

The replication of positive-strand RNA plant viruses, which involves both virus-encoded and plant-encoded proteins, takes place in two stages: synthesis of a negative-strand RNA using the genomic positive-strand RNA as a template and synthesis of progeny positive-strand RNA using the negative-strand RNA as a template. Using gel mobility shift and photochemical crosslinking assays, we have identified three proteins of M(r) 32K, 50K and 100K in extracts of tobacco and spinach leaves that bind to the 3'-terminal sequences of the negative-strand RNA of three diverse positive-strand RNA plant viruses. The 32K protein was purified to near homogeneity by chromatography on columns of Macro-prep high Q, heparin-sepharose, single-stranded DNA cellulose and poly(U)-sepharose. No binding of any of the three proteins to the 3'-termini of the positive-strand RNA or the 5'-termini of the positive-strand RNA or negative-strand RNA of any of the three viruses, or the 3'-termini of the mRNAs of two chloroplast genes, psbA or petD, could be detected. We propose that 3'-terminal negative-strand RNA binding proteins, which may be widespread in the plant kingdom, could be utilised by at least three different positive-strand RNA plant viruses for the initiation of positive-strand RNA synthesis.

Base Sequence↗
PubMedDate not supplied

Plant protein hydrolysates: preparation of defined peptide fractions promoting growth and production in animal cells cultures.

A new approach was applied with the aim at producing plant protein hydrolysates less heterogeneous and less contaminated with nonpeptide substances than are the presently available digests. A significant reduction of nonprotein contaminants was achieved by extraction of the plant material, soy flour or wheat flour, with acetone prior to isolation of the protein. Enzymes of nonanimal origin, papain or Pronase, were used for protein hydrolysis. The components of the hydrolysates were resolved by low-pressure liquid chromatography. Separation of peptide fractions and of remaining nonpeptide contaminants was achieved using small-pore size-exclusion chromatography matrices, Sephadex G-15 or Biogel P-2. Individual peptide fractions, both from soy protein and from wheat gluten, varied substantially in their growth-promoting and production-enhancing activities when tested on a mouse hybridoma culture in protein-free medium. The highest enhancement of viable cell density in batch cultures was 180% of control, and the highest enhancement of final immunoglobulin concentration was more than 230% of control. The existence of marked differences in activity of individual peptide fractions leads to a suggestion that the hydrolysates may provide peptides exerting specific positive effects on cultured animal cells.

Animals↗