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GrainGenes Reference Report: PPS-125-1732

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Reference	PPS-125-1732
Title	Pea legumin overexpressed in wheat endosperm assembles into an ordered paracrystalline matrix
Journal	Plant Physiology
Year	2001
Volume	125
Pages	1732-1742
Author	Stoger E Parker M Christou P Casey R
Abstract	Summary: 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
External Databases	Pubmed: 11299354
Keyword	[ Hide all but 1 of 35 ] bodies characterization crystal endosperm gene globulins golgi heterogeneity in vitro in vivo inclusions isolate legume localization matrix pea polypeptide posttranslational cleavage precursor prolamin seed seed storage protein single storage storage protein storage vacuoles structural-analysis tissue specific expression transgenic transgenic rice endosperm transgenic wheat triticin triticum aestivum vacuole wheat endosperm

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