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Plant Cell, Vol. 11, 1499-1508, August 1999, Copyright © 1999, American Society of Plant Physiologists

Identification and Characterization of a Prevacuolar Compartment in Stigmas of Nicotiana alata

Elizabeth A. Millera, Marcus C. S. Leea, and Marilyn A. Andersona
a School of Biochemistry, LaTrobe University, Bundoora, Victoria 3083, Australia

Correspondence to: Marilyn A. Anderson, M.Anderson{at}latrobe.edu.au (E-mail), 61-3-9479-2467 (fax)

The stigmas of the ornamental tobacco plant Nicotiana alata accumulate large quantities of a series of 6-kD proteinase inhibitors (PIs) in the central vacuole that are derived from a 40-kD precursor protein, Na-PI. The sorting information that directs Na-PI to the vacuole is likely to reside in a C-terminal propeptide domain of 25 amino acids that forms an amphipathic {alpha} helix. Using cell fractionation techniques, we have examined transit of Na-PI through the endomembrane system and have identified a prevacuolar compartment that contains Na-PI with an intact targeting signal. In contrast, the targeting signal is not present on the predominant form of Na-PI in the vacuole. The prevacuolar compartment is marked by the presence of homologs of both the t-SNARE, PEP12p, and the putative vacuolar sorting receptor BP-80. Cross-linking and affinity precipitation studies revealed that Na-PI associates with BP-80 within this compartment, providing in vivo evidence for the function of BP-80 as a sorting receptor for a protein with a C-terminal vacuolar targeting signal.


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