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Plant Physiol, April 2001, Vol. 125, pp. 1732-1742
Pea Legumin Overexpressed in Wheat Endosperm Assembles into an
Ordered Paracrystalline Matrix1
Eva
Stöger,
Mary
Parker,
Paul
Christou, and
Rod
Casey*
Molecular Biotechnology Unit (E.S., P.C.) and Department of Applied
Genetics (R.C.), John Innes Centre, Norwich Research Park, Colney Lane,
Norwich NR4 7UH, United Kingdom; and Institute of Food Research,
Norwich Research Park, Colney Lane, Norwich NR4 7UA, United Kingdom
(M.P.)
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.
1
This work was supported by The John Innes Centre
and by the Institute of Food Research, which are supported in part by a
grant-in-aid from the Biotechnology and Biological Science Research Council.
*
Corresponding author; e-mail rod.casey{at}bbsrc.ac.uk; fax
44-1603-456844.
© 2001 American Society of Plant Physiologists
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