蛋白质跨酵母微粒体膜的转运受到一种可溶性因子的刺激。
Protein translocation across the yeast microsomal membrane is stimulated by a soluble factor.
作者信息
Waters M G, Chirico W J, Blobel G
出版信息
J Cell Biol. 1986 Dec;103(6 Pt 2):2629-36. doi: 10.1083/jcb.103.6.2629.
Abstract
We have found that a soluble activity present in the postribosomal supernatant fraction of Saccharomyces cerevisiae stimulates posttranslational translocation of yeast prepro-alpha-factor across yeast microsomal membranes. Stimulation of translocation is not due to a nonspecific affect on ATP levels. The activity is likely to be due to protein(s) as it is destroyed by N-ethylmaleimide, protease, or heat treatment but not by incubation with RNase. Its apparent sedimentation coefficient is approximately 9.6 S.
摘要
我们发现，酿酒酵母核糖体后上清液组分中存在的一种可溶性活性物质能刺激酵母前原α因子跨酵母微粒体膜的翻译后转运。转运的刺激并非对ATP水平的非特异性影响所致。该活性可能归因于蛋白质，因为它会被N-乙基马来酰亚胺、蛋白酶或热处理破坏，但不会因与核糖核酸酶孵育而被破坏。其表观沉降系数约为9.6 S。
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本文引用的文献
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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.
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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。
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