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THE PLANT CELL, Vol 3, Issue 7 695-708, Copyright © 1991 by American Society of Plant Biologists
Different Legumin Protein Domains Act as Vacuolar Targeting Signals
G. Saalbach, R. Jung, G. Kunze, I. Saalbach, K. Adler and K. Muntz
Institute of Genetics and Crop Plant Research, Corrensstrasse 3, O-4325 Gatersleben, Sachsen-Anhalt, Federal Republic of Germany
Legumin subunits are synthesized as precursor polypeptides and are
transported into protein storage vacuoles in field bean cotyledons. We
expressed a legumin subunit in yeast and found that in these cells it is
also transported into the vacuoles. To elucidate vacuolar targeting
information, we constructed gene fusions of different legumin
propolypeptide segments with either yeast invertase or chloramphenicol
acetyltransferase as reporters for analysis in yeast or plant cells,
respectively. In yeast, increasing the length of the amino-terminal segment
increased the portion of invertase directed to the vacuole. Only the
complete legumin [alpha] chain (281 amino acids) directed over 90% to the
vacuole. A short carboxy-terminal legumin segment (76 amino acids) fused to
the carboxy terminus of invertase also efficiently targeted this fusion
product to yeast vacuoles. With amino-terminal legumin-chloramphenicol
acetyltransferase fusions expressed in tobacco seeds, efficient vacuolar
targeting was obtained only with the complete [alpha] chain. We conclude
that legumin contains multiple targeting information, probably formed by
higher structures of relatively long peptide sequences.
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