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蛋白质向麦芽糖假丝酵母微粒体膜的翻译后转运。

Post-translational transport of proteins into microsomal membranes of Candida maltosa.

作者信息

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

机构信息

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

出版信息

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

DOI:10.1002/j.1460-2075.1988.tb03006.x
PMID:3169003
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC457166/
Abstract

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.

摘要

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。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/f30431712f94/emboj00143-0198-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/a0107f1900f1/emboj00143-0196-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/dd59ffedc57b/emboj00143-0197-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/6b19d05f4428/emboj00143-0197-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/b35c86951545/emboj00143-0198-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/f30431712f94/emboj00143-0198-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/a0107f1900f1/emboj00143-0196-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/dd59ffedc57b/emboj00143-0197-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/6b19d05f4428/emboj00143-0197-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/b35c86951545/emboj00143-0198-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e9b6/457166/f30431712f94/emboj00143-0198-b.jpg

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本文引用的文献

1
Secretion in yeast: translocation and glycosylation of prepro-alpha-factor in vitro can occur via an ATP-dependent post-translational mechanism.酵母中的分泌：体外前原α因子的转运和糖基化可通过一种依赖ATP的翻译后机制发生。
EMBO J. 1986 May;5(5):1031-6. doi: 10.1002/j.1460-2075.1986.tb04318.x.
2
Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.蛋白质在内质网上的转运III. 信号识别蛋白（SRP）导致依赖信号序列和位点特异性的链延伸停滞，这种停滞可被微粒体膜解除。
J Cell Biol. 1981 Nov;91(2 Pt 1):557-61. doi: 10.1083/jcb.91.2.557.
3
TRiC/CCT在不同蛋白质类别的折叠过程中与不同的上游伴侣蛋白协同作用。
EMBO J. 2003 Oct 1;22(19):5230-40. doi: 10.1093/emboj/cdg483.
4
Protein transport and compartmentation in yeast.酵母中的蛋白质转运与区室化
Folia Microbiol (Praha). 1991;36(1):3-34. doi: 10.1007/BF02935819.
Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.
蛋白质在内质网上的转运。I. 信号识别蛋白（SRP）与体外组装的合成分泌蛋白的多核糖体结合。
J Cell Biol. 1981 Nov;91(2 Pt 1):545-50. doi: 10.1083/jcb.91.2.545.
4
Secretory protein translocation across membranes-the role of the "docking protein'.分泌蛋白跨膜转运——“对接蛋白”的作用
Nature. 1982 Jun 24;297(5868):647-50. doi: 10.1038/297647a0.
5
Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum.通过碳酸钠处理分离细胞内膜：应用于内质网
J Cell Biol. 1982 Apr;93(1):97-102. doi: 10.1083/jcb.93.1.97.
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Different modes of membrane interactions of the signal sequence of carp preproinsulin and of the insertion sequence of rabbit cytochrome b5.鲤鱼胰岛素原前体信号序列和兔细胞色素b5插入序列的不同膜相互作用模式。
Eur J Biochem. 1982 Mar;123(1):121-6. doi: 10.1111/j.1432-1033.1982.tb06507.x.
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