By J.A. Callow (Eds.)
Articles during this vintage Papers quantity are rewritten, up-dated and prolonged models of papers released in prior volumes of Advances in Botanical examine, selected as a result of excessive quotation of the unique papers and the rise of information within the box this present day. Boulter and Croy speak about the constitution and biosynthesis of legume seed garage proteins, a space that has been revolutionized lately by advances in three-D structural research and strategies of gene manipulation. Raven writes concerning the major development made in our figuring out of the biochemistry of inorganic carbon acqui. Read more...
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Extra resources for Classic Papers
That a relationship can be recognized between the N-terminal domain of vicilin and the acidic chain of legumin, and that vicilin and legumin can be derived from a common structural domain by duplication (see Plate 4). By starting with the observation that two residues Pro67 and Gly81 in the N-terminal domain (equivalent to Pro254 and Gly269 in the C-terminal domain) are conserved between species and between the N- and C-terminal domains of vicilin, Lawrence et al. (1994) have aligned the available vicilin and legumin sequences to show 30 sites so-called “globally conserved” across the 11s and 7s families.
E. , 1993). , 1970; see references quoted in Chrispeels, 1991). The translocation mechanism is probably similar to, but not identical with, the one in mammalian cells (Chrispeels, 1991). To give one typical example, legumin subunits are synthesized in all legumes investigated as precursor molecules (pre-prolegumin) o n the polysomes of the KER which has been co-ordinately synthesized at this time. , 1980b, 1982). The signal peptide, which has the typical eukaryotic composition and properties, is sufficient to ensure entry and it is co-translationally removed as the precursor is inserted into the lumen of the RER.
A) Quaternary structure of legumin from sunflower based on data from small-angle X-ray scattering and quasi-electric light scattering. The model shows an approximately spherical molecule with six near-identical monomers arranged in a trigonal antiprism givin an overall oblate ellipsoid shape of approximate dimensions 110 8, x 110 A x 88 . Each monomer comprises of an acidic polypeptide (40 kDa) and a smaller basic polypeptide (20 kDa). Arrows indicate three axes of symmetry. (B) Hypothetical model of the arrangement of acidic and basic chains within the legumin hexameric molecule viewed from the side of the molecule.
Classic Papers by J.A. Callow (Eds.)