Müller M, Ibrahimi I, Chang C N, Walter P, Blobel G
J Biol Chem. 1982 Oct 25;257(20):11860-3.
In vitro transcription of DNA from plasmid pBR322 was coupled to cell-free translation in a wheat germ system. The major translation product was pre-beta-lactamase. Upon addition of dog pancreas microsomes, the precursor was processed to authentic beta-lactamase as shown by partial NH2-terminal sequence analysis. Processing was linked to translocation into the microsomal vesicles. Salt-extracted microsomes did not process pre-beta lactamase but could be reactivated by purified signal recognition particle, which is the functional component of the salt wash (Walter, P., and Blobel, G. (1980) Proc. Natl. Acad. Sci. U. S. A. 77, 7112-7116). Signal recognition particle alone caused a drastic translation arrest that could be released by salt-depleted membranes. These data are consistent with those obtained for eukaryotic proteins and suggest that co-translational translocation of both bacterial and eukaryotic secretory proteins across the endoplasmic reticulum require identical components.
在小麦胚芽系统中，将质粒pBR322的DNA体外转录与无细胞翻译偶联。主要的翻译产物是前β-内酰胺酶。加入犬胰腺微粒体后，通过部分氨基末端序列分析表明，前体被加工成了真正的β-内酰胺酶。加工过程与转运到微粒体小泡中有关。盐提取的微粒体不能加工前β-内酰胺酶，但可被纯化的信号识别颗粒重新激活，信号识别颗粒是盐洗的功能成分（沃尔特，P.，和布洛贝尔，G.（1980年）美国国家科学院院刊77，7112 - 7116）。单独的信号识别颗粒会导致剧烈的翻译停滞，而这种停滞可被低盐的膜释放。这些数据与针对真核蛋白质获得的数据一致，并表明细菌和真核分泌蛋白在内质网上的共翻译转运需要相同的成分。
