Secretion of plant storage globulin polypeptides by Xenopus laevis oocytes.
Xenopus oocytes injected with poly(A)-containing RNA from developing cotyledons of field beans (Vicia faba L. var. minor) synthesize precursor polypeptides to the major storage globulins legumin and vicilin. These polypeptides are secreted into the medium without proteolytic cleavage of the legumin propolypeptides into the mature disulfide-linked alpha and beta chains. Similarly, storage globulin polypeptides from pea (Pisum sativum L.) and french bean (Phaseolus vulgaris L.) were secreted from oocytes. Inhibition of glycosylation by tunicamycin does not prevent secretion. This first report on the secretion of plant polypeptides by Xenopus oocytes shows that (a) intracellular deposition of storage proteins in membrane-bounded organelles (protein bodies) of plants and extracellular secretion have step(s) in common, and (b) the cell, in addition to the mRNA, determines the final destination of these polypeptides.
D000818:Animals; D007887:Fabaceae; D005260:Female; D005916:Globulins / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D009865:Oocytes / Q000378:metabolism*; D010063:Ovum / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D014674:Plant Proteins, Dietary / Q000378:metabolism; D010946:Plants, Medicinal; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism; D055314:Seed Storage Proteins; D014982:Xenopus laevis; D000097793:Legumins
D005916:Globulins; D008565:Membrane Proteins; D010455:Peptides; D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D012333:RNA, Messenger; D055314:Seed Storage Proteins; D000097793:Legumins; C015575:vicilin protein, plant