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A reliable system for transformation and regeneration of rice protoplasts yielding fertile transgenic plants has been established. After co-electroporation of DNAs encoding a selectable marker and the gene of interest, protoplasts are regenerated to yield fertile plants. To date more than 70 different genes of interest have been successfully introduced and their patterns of expression are being studied. As in the case of dicot plants transformed by the Ti-plasm id vector approach, integration and expression appear to be stable in the transgenic monocots over several generations. Detailed com parative studies on gene expression in rice are underway using promoters for triosephosphate isomerase, a ubiquitously expressed gene encoding a cytosolic enzyme vital in the glycolytic cycle, two genes encoding members of the cyclophilin family, peptidyl-prolyl cis-trans -isomerases that are abundant in meristematic regions and are thought to participate in the correct folding of nascent proteins, and a gene encoding a tissue (root)- specific protein. Initial analyses suggest that the spatial expression of these genes in transgenic plants, using GUS reporter constructs, appears to be very sensitive to the nature of the 3' flanking region present in the gene construct. Constructs containing a coding region for arcelin, a bean seed protein with putative anti-insecticidal properties, and others containing viral sequences that may provide novel approaches for protection against tungro and other viral infections have been introduced into rice plants.
A reliable system for transformation and regeneration of rice protoplasts yielding fertile transgenic plants has been established. After co-electroporation of DNAs encoding a selectable marker and the gene of interest, protoplasts are regenerated to yield fertile plants. To date more than 70 different genes of interest have been successfully introduced and their patterns of expression are being studied. As in the case of dicot plants transformed by the Ti-plasm id vector approach, integration and expression appear to be stable in the transgenic monocots over several generations. Detailed com parative studies on gene expression in rice are underway using promoters for triosephosphate isomerase, a ubiquitously expressed gene encoding a cytosolic enzyme vital in the glycolytic cycle, two genes encoding members of the cyclophilin family, peptidyl-prolyl cis-trans -isomerases that are abundant in meristematic regions and are thought to participate in the correct folding of nascent proteins, and a gene encoding a tissue (root)- specific protein. Initial analyses suggest that the spatial expression of these genes in transgenic plants, using GUS reporter constructs, appears to be very sensitive to the nature of the 3' flanking region present in the gene construct. Constructs containing a coding region for arcelin, a bean seed protein with putative anti-insecticidal properties, and others containing viral sequences that may provide novel approaches for protection against tungro and other viral infections have been introduced into rice plants.
Legumin, a major component of pea seed storage vacuoles, is synthesized by a number of paralogous genes. The polypeptides are cleaved posttranslationally and can form mixed hexamers. This heterogeneity hampers structural studies, based on the production of hexamer crystals in vitro. To study a single type of homogenous legumin we produced pea legumin A in transgenic wheat (Triticum aestivum) endosperm where prolamins are predominant and only small amounts of globulins accumulate in separate inclusions. We demonstrated that the legumin precursor was cleaved posttranslationally and we confirmed assembly into 11S hexamers. Legumin was deposited within specific regions of the inclusion bodies. Angular legumin crystals extended from the inclusion bodies into the vacuole, correlating with the high legumin content. This suggests that the high-level production of a single type of legumin polypeptide resulted in the spontaneous formation of crystals in vivo. The use of a heterologous cereal system such as wheat endosperm to produce, isolate, and recrystallize homogenous 11S legume globulins offers exciting possibilities for structural analysis and characterization of these important seed storage proteins.
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