By J.A. Callow (Eds.)
Articles during this vintage Papers quantity are rewritten, up-dated and prolonged types of papers released in prior volumes of Advances in Botanical study, selected as a result of the excessive quotation of the unique papers and the rise of information within the box this present day. Boulter and Croy talk about the constitution and biosynthesis of legume seed garage proteins, a space that has been revolutionized in recent times by advances in 3-D structural research and techniques of gene manipulation. Raven writes in regards to the major development made in our knowing of the biochemistry of inorganic carbon acqui. Read more...
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LEGUME SEED STORAGE PROTEINS 39 More recently, these three events have been investigated at the level of individual cotyledon cells by using fluorescence to quantify the DNA and immunofluorescence to identify vicilin. Tubulin immunofluorescence was used to monitor the state of the cytoskeleton. I n situ hybridization using tritium-labelled sense and antisense cDNA sequences was used to follow the cellular expression of the vicilin and legumin genes. From these studies (see details in Wang and Hedley, 1993) it was concluded that storage protein gene expression occurred only in ceHs lacking mitotic activity.
However, Harris et al. (1989) have shown that at least one legumin gene is active and that legumin protein is transitorily produced in the coenocytic endosperm tissue of the globular stage pea embryo (early maturation stage). More recently and more extensively, Wobus et al. (1995) have shown that legumin mRNA and protein are transiently accumulated during early embryogenesis, and that legumin expression is not embryo-specific nor restricted to the cell expansion phase of seed development. Thus, in faba bean, vicilin and legumin storage proteins are synthesized early in development in the suspensor, the endosperm and globular storage embryos, and in parenchyma cells of the maternal seed coat at specific stages for each tissue before their final large accumulation in the cotyledon-stage embryos.
SECONDARY, TERTIARY AND QUATERNARY STRUCTURE Narbonin is the only available example of the 2 s globulins of legumes whose three-dimensional structure has been determined at high resolution. , 1990). The size of the molecule is 45 A X 45 A X 30 A and it comprises a single domain folded into a compact eight-stranded culp barrel, which is structurally analogous to triose phosphate isomerase (TIM), hence its description as a TIM barrel protein. The main feature of the protein is the eight-stranded parallel P-barrel, which forms the core of the molecule with seven a-helices packed around it.