体外合成与加工大肠杆菌碱性磷酸酶前体
Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro.
作者信息
Inouye H, Beckwith J
出版信息
Proc Natl Acad Sci U S A. 1977 Apr;74(4):1440-4. doi: 10.1073/pnas.74.4.1440.
Abstract
Alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] of E. coli was synthesized in a cell-free system, and the size of the direct translation product was analyzed. The product has a higher molecular weight than the mature alkaline phosphatase found in the periplasm. The direct translation product can be processed to the mature size by an E. coli membrane fraction; the processing activity copurifies with the outer-membrane fraction. The presumed precursor can dimerize to form active enzyme without being processed, and the resultant enzyme appears to be more hydrophobic than the mature enzyme. These findings are discussed in connection with the "signal hypothesis" proposed for the excretion of proteins across membranes.
摘要
大肠杆菌的碱性磷酸酶[正磷酸单酯磷酸水解酶（最适pH为碱性），EC 3.1.3.1]在无细胞系统中合成，并对直接翻译产物的大小进行了分析。该产物的分子量高于周质中发现的成熟碱性磷酸酶。直接翻译产物可被大肠杆菌膜组分加工成成熟大小；加工活性与外膜组分共纯化。推测的前体可以在不被加工的情况下二聚化形成活性酶，并且所得的酶似乎比成熟酶更疏水。结合提出的关于蛋白质跨膜分泌的“信号假说”对这些发现进行了讨论。
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