Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 96:18-25 (1991)
© 1991 American Society of Plant Biologists

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Cellular and Structural Biology

The Signal Peptide of a Vacuolar Protein Is Necessary and Sufficient for the Efficient Secretion of a Cytosolic Protein 1

Dale C. Hunt and Maarten J. Chrispeels

Department of Biology and Center for Molecular Genetics, University of California, San Diego, La Jolla, California 92093-0116

A cytosolic pea (Pisum sativum) seed albumin (ALB) and a chimeric protein (PHALB) consisting of the signal peptide and first three amino acids of phytohemagglutinin (PHA) and the amino acid sequence of ALB were expressed in parallel suspension cultures of tobacco (Nicotiana tabacum) cells and their intracellular fates examined. PHALB was efficiently secreted by the cells whereas ALB remained intracellular. These experiments show that the information contained in the signal peptide of a vacuolar protein is both necessary and sufficient for efficient secretion, and define secretion as a default or bulk-flow pathway. Entry into the secretory pathway was accompanied by glycosylation and the efficient conversion of the high mannose glycans into complex glycans indicating that transported glycoproteins do not need specific recognition domains for the modifying enzymes in the Golgi. Tunicamycin depressed the accumulation of the unglycosylated polypeptide in the culture medium much less than the accumulation of other glycoproteins. We interpret this as evidence that glycans on proteins that are not normally glycosylated do not have the same function of stabilizing and protecting the polypeptide as on natural glycoproteins.

1 Supported by a grant from the National Science Foundation (Cell Biology) and a contract from the United States Department of Energy (Basic Energy Biosciences).




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