RT Journal Article
SR Electronic
T1 Interaction of a Potential Vacuolar Targeting Receptor with Amino- and Carboxyl-Terminal Targeting Determinants
JF Plant Physiology
JO Plant Physiol.
FD American Society of Plant Biologists
SP 469
OP 474
DO 10.1104/pp.111.2.469
VO 111
IS 2
A1 Kirsch, T.
A1 Saalbach, G.
A1 Raikhel, N. V.
A1 Beevers, L.
YR 1996
UL http://www.plantphysiol.org/content/111/2/469.abstract
AB 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.