哺乳动物微粒体对细菌前β-内酰胺酶的转运与切割
Transport and cleavage of bacterial pre-beta-lactamase by mammalian microsomes.
作者信息
Kronenberg H M, Fennick B J, Vasicek T J
出版信息
J Cell Biol. 1983 Apr;96(4):1117-9. doi: 10.1083/jcb.96.4.1117.
Abstract
Eucaryotic endoplasmic reticulum and bacterial inner cell membranes use strikingly similar mechanisms to transport proteins from one cellular compartment to another. Using a mammalian linked transcription-translation system, we show here that canine pancreatic microsomes accurately cleave off the signal sequence of beta-lactamase, a secreted bacterial protein. We suggest that the apparent differences between bacterial and eukaryotic protein transport may involve only minor modulations of a profoundly conserved mechanism.
摘要
真核生物的内质网和细菌的内膜利用极为相似的机制将蛋白质从一个细胞区室转运到另一个细胞区室。我们利用哺乳动物的转录-翻译偶联系统，在此表明犬胰腺微粒体能准确切割掉分泌型细菌蛋白β-内酰胺酶的信号序列。我们认为，细菌和真核生物蛋白质转运之间明显的差异可能仅涉及对一种高度保守机制的微小调节。
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本文引用的文献
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Maize chloroplast DNA fragment encoding the large subunit of ribulosebisphosphate carboxylase.编码核酮糖二磷酸羧化酶大亚基的玉米叶绿体DNA片段。
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Transfer of proteins across membranes.蛋白质跨膜转运
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Bacteria mature preproinsulin to proinsulin.细菌将前胰岛素原成熟为胰岛素原。
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Secretion of beta-lactamase requires the carboxy end of the protein.β-内酰胺酶的分泌需要该蛋白质的羧基末端。
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A mechanism of protein localization: the signal hypothesis and bacteria.蛋白质定位机制：信号假说与细菌
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