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THE PLANT CELL, Vol 6, Issue 12 1911-1922, Copyright © 1994 by American Society of Plant Biologists
Two Structural Domains Mediate Two Sequential Events in [gamma]-Zein Targeting: Protein Endoplasmic Reticulum Retention and Protein Body Formation
M. I. Geli, M. Torrent and D. Ludevid
Departamento de Genetica Molecular, Centro de Investigacion y Desarrollo de Barcelona, Consejo Superior de Investigaciones Cientificas, C/ Jorge Girona Salgado 18-26, 08034 Barcelona, Spain
[gamma]-Zein is a maize storage protein synthesized by endosperm cells and
stored together with [alpha]- and [beta]-zeins in specialized organelles
called protein bodies. Previous studies have shown that in maize there is
only one type of protein body and it is derived directly from the
endoplasmic reticulum (ER). In this article, we describe the domains of
[gamma]-zein involved in ER retention and the domains involved in protein
body formation. To identify the signal responsible for [gamma]-zein
retention in ER-derived protein bodies, DNAs encoding various deletion
mutants of [gamma]-zein were constructed and introduced into Arabidopsis as
a heterologous system. By using pulse-chase experiments and immunoelectron
microscopy, we demonstrated that the deletion of a proline-rich domain at
the N terminus of [gamma]-zein puts an end to its retention in the ER; this
resulted in the secretion of the mutated protein. The amino acid sequence
of [gamma]-zein necessary for ER retention is the repeat domain composed of
eight units of the hexapeptide PPPVHL. In addition, we observed that only
those [gamma]-zein mutants that contained both the proline-rich repeat
domain and the C-terminal cysteine-rich domain were able to form ER-derived
protein bodies. We suggest that the retention of [gamma]-zein in the ER
could be a result of a protein-protein association or a transient
interaction of the repeat domain with ER membranes.
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