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• W2146275330 endingPage "390" @default.
• W2146275330 startingPage "381" @default.
• W2146275330 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." @default.
• W2146275330 created "2016-06-24" @default.
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• W2146275330 creator A5029599635 @default.
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• W2146275330 date "1989-03-01" @default.
• W2146275330 modified "2023-09-23" @default.
• W2146275330 title "Endoplasmic reticulum targeting and glycosylation of hybrid proteins in transgenic tobacco." @default.
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• W2146275330 doi "https://doi.org/10.1105/tpc.1.3.381" @default.
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• W2146275330 hasPublicationYear "1989" @default.
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