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. 1989 Mar;1(3):381–390. doi: 10.1105/tpc.1.3.381

Endoplasmic reticulum targeting and glycosylation of hybrid proteins in transgenic tobacco.

G Iturriaga 1, R A Jefferson 1, M W Bevan 1
PMCID: PMC159770  PMID: 2535509

Abstract

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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Selected References

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