Bassüner R, Wobus U, Rapoport T A
FEBS Lett. 1984 Jan 30;166(2):314-20. doi: 10.1016/0014-5793(84)80103-9.
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.
对编码蚕豆（野豌豆）单个贮藏球蛋白多肽的杂交选择mRNA在无细胞系统中进行翻译。添加的哺乳动物信号识别颗粒（SRP）识别主要豌豆球蛋白和两种豆球蛋白多肽前体的可裂解信号肽，并诱导翻译停滞。后者可被经钾洗涤的膜（K-RM）释放，从而产生受蛋白酶保护的缩短多肽。因此，SRP和K-RM对植物多肽的作用方式与对哺乳动物分泌蛋白所描述的相似[（1981年）《细胞生物学杂志》91卷，557 - 561页]。显然，植物贮藏球蛋白多肽生物合成和加工的初始步骤与动物分泌蛋白的基本相同。
