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globulin/arabidopsis

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Disulfide interchange reactions in 11S globulin subunits of Cruciferae seeds. Relationships to gene families.

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Cruciferin, the main storage protein in rapeseed (Brassica napus L.), is a legumin-like 11S globulin. Using SDS/PAGE cruciferin was shown to be composed of different subunits consisting of alpha S and beta S polypeptides, which were disulfide linked, and also closely related free alpha f and beta f

Characterization of the 12S globulin complex of Brassica napus. Evolutionary relationship to other 11-12S storage globulins.

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Cruciferin (12S globulin) is the major seed protein in Brassica napus (oil seed rape). It is synthesized during seed development and consists of six subunit pairs. Each of these pairs is synthesized as a precursor containing one alpha and one beta chain. At least three different precursors exist
This study investigated the subcellular location of mung bean (Vigna radiata) 8S globulin in transient expression systems as well as in tobacco (Nicotiana tabacum) BY-2 cells and different tissues from a transgenic Arabidopsis (Arabidopsis thaliana) line stably expressing this storage globulin. When

Expression and characterization of the Arabidopsis thaliana 11S globulin family.

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The 11S globulins are the principal seed storage proteins in a variety of major crop species, including members of the legume and mustard families. They are targets for protein engineering studies attempting to alter the physicochemical properties of seed protein extracts (e.g. soybean) and to
Nanobody-heavy chain (VHH-Fc) antibody formats have the potential to immunomodulate even highly accumulating proteins and provide a valuable tool to experimentally modulate the subcellular distribution of seed storage proteins. Recombinant antibodies often obtain high accumulation levels in plants,

Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds.

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Cruciferin (a 12 S globulin) is the most abundant storage protein in the seeds of Arabidopsis thaliana (thale cress) and other crucifers, sharing structural similarity with the cupin superfamily of proteins. Cruciferin is synthesized as a precursor in the rough endoplasmic reticulum. Subunit

Cotton alpha-globulin promoter: isolation and functional characterization in transgenic cotton, Arabidopsis, and tobacco.

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Globulins are the most abundant seed storage proteins in cotton and, therefore, their regulatory sequences could potentially provide a good source of seed-specific promoters. We isolated the putative promoter region of cotton alpha-globulin B gene by gene walking using the primers designed from a
Vacuolar sorting of seed storage proteins is a very complex process since several sorting pathways and interactions among proteins of different classes have been reported. In addition, although the C-terminus of several 7S proteins is important for vacuolar delivery, other signals seem also to be

A Vigna radiata 8S globulin α' promoter drives efficient expression of GUS in Arabidopsis cotyledonary embryos.

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Plants are proven effective bioreactors for the production of heterologous proteins including those desired by the biopharmaceutical industry. However, the potential of plants as bioreactors is limited by the availability of characterized plant promoters that can drive target gene expression in
Sulfate is required for the synthesis of sulfur-containing amino acids and numerous other compounds essential for the plant life cycle. The delivery of sulfate to seeds and its translocation between seed tissues is likely to require specific transporters. In Arabidopsis (Arabidopsis thaliana), the
Seed storage proteins are synthesized as sources of carbon, nitrogen and sulfur for the next generation of plants. Their composition changes according to nutritional conditions. Here, we report the precise molecular identification of seed proteins by proteomic analysis of wild-type Arabidopsis

Strong seed-specific protein expression from the Vigna radiata storage protein 8SGα promoter in transgenic Arabidopsis seeds.

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Vigna radiata (mung bean) is an important crop plant and is a major protein source in developing countries. Mung bean 8S globulins constitute nearly 90% of total seed storage protein and consist of three subunits designated as 8SGα, 8SGα' and 8SGβ. The 5'-flanking sequences of 8SGα' has been

Two naturally occurring deletion mutants of 12S seed storage proteins in Arabidopsis thaliana.

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Two naturally occurring Arabidopsis mutants, Cape Verde Islands and Monte (Mr-0), with aberrant 12S seed storage protein (SSP) profiles have been identified by SDS-PAGE. In both mutants, one of the 12S globulin bands is missing while a new band of lower molecular mass is present. Tandem mass

MAIGO2 is involved in exit of seed storage proteins from the endoplasmic reticulum in Arabidopsis thaliana.

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Seed storage proteins are synthesized on the endoplasmic reticulum (ER) as precursors and then transported to protein storage vacuoles, where they are processed into mature forms. Here, we isolated an Arabidopsis thaliana mutant, maigo2 (mag2), that accumulated the precursors of two major storage

Molecular cloning, genomic organization, expression and evolution of 12S seed storage protein genes of Arabidopsis thaliana.

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We have identified a number of genes of the flowering plant Arabidopsis thaliana that are abundantly expressed during embryogenesis. In this paper we discuss four of these genes, which comprise a gene family: complete genomic nucleotide sequence of two of the genes and partial sequence of the other
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