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The Arabidopsis thaliana (At) 2S albumin gene 3 (At2S3) has been cloned in YEp13 as a 3.5-kb genomic fragment. To study its expression in Saccharomyces cerevisiae, the accumulation in saturated cultures reached about 0.032% of the yeast total protein, and the product was localized in vacuolar bodies
With the aim of increasing the rumen-protected level of the sulphur amino acids cysteine and methionine in Trifolium repens, we introduced the coding sequence of the sunflower seed albumin (SSA) into T. repens by Agrobacterium tumefaciens-mediated transformation. The SSA gene was modified such that
Two genes, BE2S1 and BE2S2, coding for methionine-rich albumins of Brazil nut (Bertholletia excelsa H.B.K.) have been cloned and their sequence determined. The genes are members of a multigene family and one of them, i.e. BE2S1, codes for one of the dominant 2S isoforms. Its expression is highly
The 2S albumin genes of Arabidopsis thaliana are a model system to study gene expression during late embryogenesis. The at2S1 gene has previously been shown to be expressed essentially in the embryo axis, unlike at2S2, which is expressed throughout the embryo. Hybrid promoter constructs between
2S albumin seed storage proteins undergo a complex series of posttranslational proteolytic cleavages. In order to determine if this process is correctly carried out in transgenic plants, the gene AT2S1 encoding an Arabidopsis thaliana 2S albumin isoform has been expressed in transgenic tobacco.
To investigate the possible roles of the Arabidopsis thaliana 2S albumin propeptides with respect to sorting, processing, and stability of the protein in plant cells, five gene constructions deleting or modifying the propeptides were made based on one of the genes encoding the Arabidopsis 2S
The Arabidopsis thaliana 2 S albumins are examples of vacuolar proteins which undergo intensive posttranslational processing. An in vitro processing assay to screen for processing enzymes present in seeds was developed using an in vitro synthesized 2 S albumin precursor as the substrate. A protease
The most abundant isoform of the 2S albumin present in seeds of Arabidopsis thaliana has been sequenced and the corresponding gene isolated. Examination of the protein and DNA sequences allows the determination of the exact proteolytic cleavage sites during posttranslational processing. Like other
We studied the expression of the four genes encoding 2S albumin seed storage proteins (at2S1 to at2S4) in Arabidopsis thaliana. All four genes followed similar temporal profiles throughout development, but at2S2 and at2S3 were expressed at significantly higher levels than at2S1 or at2S4. In situ
We have previously reported that precursor-accumulating (PAC) vesicles found exclusively in developing seeds are involved in a transport of seed storage proteins, such as 2S albumin, from the endoplasmic reticulum to protein-storage vacuoles. Here, we constructed chimeric genes that encode fusion
Genetic and molecular studies have shown that the Arabidopsis ABSCISIC ACID-INSENSITIVE3 (ABI3) protein plays a prominent role in the control of seed maturation. The ABI3 protein and its orthologues from various other plant species share four domains of high sequence identity, including three basic
Soluble proteins reach vacuoles because they contain vacuolar sorting determinants (VSDs) that are recognized by vacuolar sorting receptor (VSR) proteins. Pre-vacuolar compartments (PVCs), defined by VSRs and GFP-VSR reporters in tobacco BY-2 cells, are membrane-bound intermediate organelles that
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
The low level of methionine, an essential sulfur-containing amino acid, limits the nutritional quality of seeds. Two main factors can control the level of protein-bound methionine: the level of free methionine that limits protein accumulation and the methionine residues inside the storage proteins.