蛋白质向麦芽糖假丝酵母微粒体膜的翻译后转运。

Wiedmann M, Wiedmann B, Voigt S, Wachter E, Müller H G, Rapoport T A

Zentralinstitut für Molekularbiologie, Akademie der Wissenschaften der DDR, Berlin-Buch.

EMBO J. 1988 Jun;7(6):1763-8. doi: 10.1002/j.1460-2075.1988.tb03006.x.

We have isolated from the yeast Candida maltosa microsomal membranes that are active in the translocation of proteins synthesized in cell-free systems derived from C. maltosa, Saccharomyces cerevisiae or wheat germ. Translocation and core glycosylation of prepro-alpha-factor, a secretory protein, were observed with yeast microsomes added during or after translation. The signal peptide is cleaved off. Cytochrome P-450 from C. maltosa, the first integral membrane protein studied in a yeast system, is also inserted both co- and post-translationally into Candida microsomal membranes. Its insertion into canine microsomes occurs efficiently only in a co-translational manner and is dependent on the function of the signal recognition particle.

我们从麦芽糖假丝酵母中分离出了微粒体膜，这些膜在源自麦芽糖假丝酵母、酿酒酵母或小麦胚芽的无细胞系统中合成的蛋白质转运过程中具有活性。在翻译过程中或翻译后添加酵母微粒体时，可观察到分泌蛋白前原α因子的转运和核心糖基化。信号肽被切除。麦芽糖假丝酵母的细胞色素P-450是在酵母系统中研究的首个整合膜蛋白，它也在翻译过程中和翻译后插入到假丝酵母微粒体膜中。它仅以共翻译的方式有效地插入犬微粒体中，并且依赖于信号识别颗粒的功能。