Bonatti S, Migliaccio G, Blobel G, Walter P
Eur J Biochem. 1984 May 2;140(3):499-502. doi: 10.1111/j.1432-1033.1984.tb08130.x.
We have investigated the role of signal recognition particle (SRP) in the biosynthesis of Sindbis glycoproteins by translating the viral 26S mRNA in a wheat-germ cell-free system. SRP was shown to have no effect on the synthesis or proteolytic processing of the cytoplasmic C protein. In contrast, the membrane integration and the proteolytic processing of the viral glycoproteins PE2 and E1 were demonstrated to be SRP-dependent. In the absence of microsomal membranes, SRP caused an arrest of the synthesis of the viral glycoproteins. This arrest could be released by the addition of salt-extracted microsomal membranes. Synchronization experiments indicated that the uncleaved signal sequence of PE2 was recognized by SRP after at most 130 amino acids of PE2 had been polymerized. No apparent interaction of SRP with a putative signal sequence of E1 and/or a 6-kDa peptide could be detected.
我们通过在麦胚无细胞系统中翻译病毒26S mRNA，研究了信号识别颗粒（SRP）在辛德毕斯糖蛋白生物合成中的作用。结果表明，SRP对细胞质C蛋白的合成或蛋白水解加工没有影响。相反，病毒糖蛋白PE2和E1的膜整合及蛋白水解加工被证明依赖于SRP。在没有微粒体膜的情况下，SRP导致病毒糖蛋白合成停滞。添加盐提取的微粒体膜可解除这种停滞。同步实验表明，PE2未切割的信号序列在PE2最多聚合130个氨基酸后被SRP识别。未检测到SRP与E1的假定信号序列和/或6 kDa肽之间有明显相互作用。
