The Accumulation of ±-Zein in Transgenic Tobacco Endosperm is Stabilized by Co-expression of ²-Zein

The cysteine-poor ±-zein is the major prolamin storage protein fraction in maize endosperm and is localized in the interior of protein bodies with ´-zein, whereas the hydrophobic cysteine-rich ²- and ³-zein are found on the exterior of the PB. In transgenic tobacco endosperm expressing zein genes, ±...

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Published inPlant and cell physiology Vol. 45; no. 7; p. 864
Main Authors Coleman, Craig E, Yoho, Paula Randall, Escobar, Sonja, Ogawa, Masahiro
Format Journal Article
LanguageEnglish
Published Oxford Oxford Publishing Limited (England) 15.07.2004
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Abstract The cysteine-poor ±-zein is the major prolamin storage protein fraction in maize endosperm and is localized in the interior of protein bodies with ´-zein, whereas the hydrophobic cysteine-rich ²- and ³-zein are found on the exterior of the PB. In transgenic tobacco endosperm expressing zein genes, ±-zein was unstable unless co-expressed with ³-zein. Here we showed that ±-zein was also stabilized by ²-zein. Small accretions of ±- and ²-zeins, similar in appearance to maize protein bodies, were localized to the endoplasmic reticulum within tobacco endosperm cells. The zein proteins were also localized to protein storage vacuoles in a more dispersed pattern, suggesting that they were transported there after they were post-translationally sequestered into the ER.
AbstractList The cysteine-poor ±-zein is the major prolamin storage protein fraction in maize endosperm and is localized in the interior of protein bodies with ´-zein, whereas the hydrophobic cysteine-rich ²- and ³-zein are found on the exterior of the PB. In transgenic tobacco endosperm expressing zein genes, ±-zein was unstable unless co-expressed with ³-zein. Here we showed that ±-zein was also stabilized by ²-zein. Small accretions of ±- and ²-zeins, similar in appearance to maize protein bodies, were localized to the endoplasmic reticulum within tobacco endosperm cells. The zein proteins were also localized to protein storage vacuoles in a more dispersed pattern, suggesting that they were transported there after they were post-translationally sequestered into the ER.
Author Yoho, Paula Randall
Escobar, Sonja
Coleman, Craig E
Ogawa, Masahiro
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