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Plant Cell, Vol. 10, 825-836, May 1998, Copyright © 1998, American Society of Plant Physiologists

Transport of Storage Proteins to Protein Storage Vacuoles Is Mediated by Large Precursor-Accumulating Vesicles

Ikuko Hara-Nishimuraa,b, Tomoo Shimadaa, Kyoko Hatanoa,c, Yuka Takeuchia, and Mikio Nishimuraa,b
a Department of Cell Biology, National Institute for Basic Biology, Okazaki 444, Japan
b Department of Molecular Biomechanics, School of Life Science, Graduate University for Advanced Studies, Okazaki 444, Japan
c Faculty of Integrated Human Studies, Kyoto University, Kyoto 606-01, Japan

Correspondence to: Ikuko Hara-Nishimura, ihnishi{at}nibb.ac.jp (E-mail), 81-564-55-7505 (fax).

Novel vesicles that accumulate large amounts of proprotein precursors of storage proteins were purified from maturing pumpkin seeds. These vesicles were designated precursor-accumulating (PAC) vesicles and had diameters of 200 to 400 nm. They contained an electron-dense core of storage proteins surrounded by an electron-translucent layer, and some vesicles also contained small vesicle-like structures. Immunocytochemical analysis revealed numerous electron-dense aggregates of storage proteins within the endoplasmic reticulum. It is likely that these aggregates develop into the electron-dense cores of the PAC vesicles and then leave the endoplasmic reticulum. Immunocytochemical analysis also showed that complex glycans are associated with the peripheral region of PAC vesicles but not the electron-dense cores, indicating that Golgi-derived glycoproteins are incorporated into the PAC vesicles. These results suggest that the unique PAC vesicles might mediate a transport pathway for insoluble aggregates of storage proteins directly to protein storage vacuoles.




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