PMID: 9177320May 1, 1997Paper

Lysine-rich modified gamma-zeins accumulate in protein bodies of transiently transformed maize endosperms

Plant Molecular Biology
Margarita TorrentD. Ludevid

Abstract

During maize seed development, endosperm cells synthesize large amounts of storage proteins, alpha-, beta-, and gamma-zeins, which accumulate within endoplasmic reticulum (ER)-derived protein bodies. The absence of lysine in all zein polypeptides results in an imbalance in the amino acid composition of maize seeds. We modified the maize gamma-zein gene through the introduction of lysine-rich (Pro-Lys)n coding sequences at different sites of the gamma-zein coding sequence. Maize endosperms were transiently transformed by biolistic bombardment with Lys-rich gamma-zein constructs under the control of the 1.7 kb gamma-zein seed-specific promoter and the cauliflower mosaic virus (CaMV) 35S promoter. When (Pro-Lys)n sequences were inserted contiguous to or in substitution of the Pro-Xaa region of the gamma-zein, high levels of protein were observed. In contrast, when (Pro-Lys)n sequences were inserted five residues from the C-terminal, the transcript was present but modified protein was not detected. These results suggest that only an appropriate positioning of Lys-rich inserts leads to the modified molecule displaying correct folding and stability. Subcellular localization analyses and immunoelectron microscopy studies on isolated p...Continue Reading

Citations

May 27, 2010·Plant Biotechnology Journal·Joseph BootheMaurice M Moloney
Apr 2, 2008·Plant Molecular Biology·Pau MarzábalM Dolores Ludevid
Mar 23, 2017·International Journal of Food Sciences and Nutrition·Xiaozhe QiKunlun Huang
Nov 10, 1998·The Plant Journal : for Cell and Molecular Biology·P MarzábalM Torrent
Jul 8, 2014·Frontiers in Plant Science·David R Holding
Feb 13, 2013·Journal of the Science of Food and Agriculture·Maozhi TangKunlun Huang

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