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PLANT PHYSIOLOGY , Vol 111, Issue 2 469-474, Copyright © 1996 by American Society of Plant Biologists

CELL BIOLOGY AND SIGNAL TRANSDUCTION

Interaction of a Potential Vacuolar Targeting Receptor with Amino- and Carboxyl-Terminal Targeting Determinants

T. Kirsch, G. Saalbach, N. V. Raikhel and L. Beevers
Department of Botany and Microbiology, University of Oklahoma, Norman, Oklahoma 73019 (T.K., L.B.)

A protein of 80 kD from developing pea (Pisum sativum) cotyledons has previously been shown to exhibit characteristics of a vacuolar targeting receptor by means of its affinity for the amino-terminal vacuolar targeting sequence of proaleurain from barley (Hordeum vulgare). In this report we show that the same protein also binds to the amino-terminal targeting peptide of prosporamin from sweet potato (lpomoea batatas) and to the carboxyl-terminal targeting determinant of pro-2S albumin from Brazil nut (Bertholletia excelsa). The receptor protein does not bind to the carboxyl-terminal propeptide (representing the targeting sequence) of barley lectin. The binding of the 80-kD protein to the sporamin determinant involves a motif (NPIR) that has been shown to be crucial for vacuolar targeting in vivo. The binding to the carboxyl-terminal targeting determinant of pro-2S albumin appears to involve the carboxyl-terminal propeptide and the adjacent five amino acids of the mature protein. The 80-kD protein does not bind to peptide sequences that have been shown to be incompetent in directing vacuolar targeting.


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Copyright © 1996 by the American Society of Plant Biologists