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.
Included in
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.
