Pea legumin overexpressed in wheat endosperm assembles into an ordered paracrystalline matrix.

@article{Stger2001PeaLO,
  title={Pea legumin overexpressed in wheat endosperm assembles into an ordered paracrystalline matrix.},
  author={Eva Maria St{\"o}ger and Mary Jo Parker and Paul Christou and Rod Casey},
  journal={Plant physiology},
  year={2001},
  volume={125 4},
  pages={1732-42}
}
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… CONTINUE READING
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