Signal recognition particle triggers the translocation of storage globulin polypeptides from field beans (Vicia faba L.) across mammalian endoplasmic reticulum membrane

FEBS Letters

Bassüner, Ronald¹  Rapoport, Tom A.²  Wobus, Ulrich¹ 

[1] Akademie der Wissenschaften der DDR, Zentralinstitut für Genetik und Kulturpflanzenforschung, DDR-4325 Gatersleben, GDR;Zentralinstitut für Molekularbiologie, DDR-1115 Berlin-Buch, GDR

关键词: Plant storage globulin polypeptide;    Cell-free translation of individual mRNA species;    Signal peptide;    Signal recognition particle;    Microsomal membrane;    Cotranslational processing;    ER;    endoplasmic reticulum;    RER;    rough endoplasmic reticulum;    hPL;    human placental lactogen;    PMSF;    phenylmethylsulfonyl fluoride;    RM;    rough microsomes;    K-RM;    potassium-washed rough microsomes;    SRP;    signal recognition particle;   

DOI  :  10.1016/0014-5793(84)80103-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown