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THE PLANT CELL, Vol 1, Issue 3 381-390, Copyright © 1989 by American Society of Plant Biologists

RESEARCH ARTICLES

Endoplasmic Reticulum Targeting and Glycosylation of Hybrid Proteins in Transgenic Tobacco

G. Iturriaga, R. A. Jefferson and M. W. Bevan
Institute of Plant Science Research, Cambridge Laboratory, Cambridge CB2 2JB, United Kingdom

The correct compartmentation of proteins to the endomembrane system, mitochondria, or chloroplasts requires an amino-terminal signal peptide. The major tuber protein of potato, patatin, has a signal peptide in common with many other plant storage proteins. When the putative signal peptide of patatin was fused to the bacterial reporter protein [beta]-glucuronidase, the fusion proteins were translocated to the endoplasmic reticulum in planta and in vitro. In addition, translocated [beta]-glucuronidase was modified by glycosylation, and the signal peptide was correctly processed. In the presence of an inhibitor of glycosylation, tunicamycin, the enzymatically active form of [beta]-glucuronidase was assembled in the endoplasmic reticulum. This is the first report of targeting a cytoplasmic protein to the endoplasmic reticulum of plants using a signal peptide.


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