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Plant Physiology 77:495-498 (1985)
© 1985 American Society of Plant Biologists

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Posttranslational Processing of Proteins in Vacuoles and Protein Bodies Is Inhibited by Monensin 1

Hetty M. Stinissen, Willy J. Peumans and Maarten J. Chrispeels

Laboratorium voor Plantenbiochemie, KULeuven, Kardinaal Mercierlaan, 92, 3030 Leuven, Belgium, Department of Biology C-016, University of California, San Diego, La Jolla, California 92093

A number of proteins that accumulate in vacuoles and protein bodies undergo posttranslational processing at these accumulation sites. These processing steps include proteolytic cleavage (e.g. pea lectin, soybean glycinin, and rice lectin) and the removal of some sugar residues from oligosaccharide side-chains (e.g. bean phytohemagglutinin). Treatment of immature rice embryos with the sodium ionophore monensin slows down the proteolytic processing of the rice lectin precursor (Mr 23,000) to mature rice lectin (Mr 10,000 and 8,000). Treatment of developing bean cotyledons with monensin slows down the removal of peripheral N-acetylglucosamine residues from the oligosaccharide side-chains of phytohemagglutinin. The results are consistent with the interpretation that these processing steps, which occur in vacuoles or protein bodies, are carried out by enzymes with an acidic pH optimum, and that monensin slows down processing by alkalinization of the vacuoles or protein bodies.

1 Supported by research grants from the National Science Foundation and the United States Department of Agriculture to M.J.C., from the NFWO to W.P., and from the WONL to H.S.




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