Theme 17: Opportunities in Molecular Biology

Description

Accumulation of zeins, the endosperm storage proteins of maize, in a heterologous plant expression system was attempted. Plants of birdsfoot trefoil (Lotus corniculatus) and alfalfa (Medicago sativa) were transformed by Agrobacterium with binary vectors harboring genes that code for γ-zein and β-zein, two proteins rich in sulphur amino acids. Adding the ER retention signal KDEL to the C-terminal domain modified zein polypeptides. Our long-term goal was to improve birdsfoot trefoil and alfalfa forage quality. Significant levels of γ- zein:KDEL and β-zein:KDEL were detected in primary transformants of birdsfoot trefoil. Moreover, alfalfa plants expressing γ-zein:KDEL in the leaves were obtained. γ-zein:KDEL accumulated in spherical or elliptical electron-dense bodies of birdsfoot trefoil leaves. The protein bodies were present in the cytoplasm of either mesophyll cells or epidermis cells.

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Accumulation of Mutated Maize Zeins in Transgenic Forage Legumes

Accumulation of zeins, the endosperm storage proteins of maize, in a heterologous plant expression system was attempted. Plants of birdsfoot trefoil (Lotus corniculatus) and alfalfa (Medicago sativa) were transformed by Agrobacterium with binary vectors harboring genes that code for γ-zein and β-zein, two proteins rich in sulphur amino acids. Adding the ER retention signal KDEL to the C-terminal domain modified zein polypeptides. Our long-term goal was to improve birdsfoot trefoil and alfalfa forage quality. Significant levels of γ- zein:KDEL and β-zein:KDEL were detected in primary transformants of birdsfoot trefoil. Moreover, alfalfa plants expressing γ-zein:KDEL in the leaves were obtained. γ-zein:KDEL accumulated in spherical or elliptical electron-dense bodies of birdsfoot trefoil leaves. The protein bodies were present in the cytoplasm of either mesophyll cells or epidermis cells.