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Signal recognition particle triggers the translocation of storage globulin polypeptides from field beans ( Vicia faba L.) across mammalian endoplasmic reticulum membrane
Author(s) -
Bassüner Ronald,
Wobus Ulrich,
Rapoport Tom A.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80103-9
Subject(s) - vicilin , vicia faba , signal peptide , endoplasmic reticulum , storage protein , legumin , biochemistry , secretory protein , signal recognition particle , globulin , biology , proteases , membrane protein , protein biosynthesis , membrane , chemistry , microbiology and biotechnology , gene , peptide sequence , botany , enzyme , immunology
Hybridization‐selected mRNAs coding for individual storage globulin polypeptides of field beans ( Vicia faba L.) were translated in a cell‐free system. Added mammalian signal recognition particle (SRP) recognizes cleavable signal peptides of the major vicilin and both legumin polypeptide precursors and induces translational arrest. The latter can be released by potassium‐washed membranes (K‐RM) leading to shortened polypeptides protected against proteases. Thus, SRP and K‐RM function in a similar way with plant polypeptides as described for mammalian secretory proteins [(1981) J. Cell Biol. 91, 557–561]. Obviously, the initial steps in the biosynthesis and processing of plant storage globulin polypeptides are principally identical to those of animal secretory proteins.