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首页> 外文期刊>Journal of bacteriology >Synthesis of R-plasmid-coded beta-lactamase in minicells and in an in vitro system.
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Synthesis of R-plasmid-coded beta-lactamase in minicells and in an in vitro system.

机译：小细胞和体外系统中R质粒编码的β-内酰胺酶的合成。

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摘要

beta-Lactamase encoded by a small, nontransferring R-plasmid, NTP1, conferring ampicillin resistance to its host bacteria, was purified. NTP1 plasmid-coded beta-lactamase was found to be periplasmically located in the host Escherichia coli cell, to have a molecular weight of about 25,000, and to show a relatively low activity against oxacillin and methicillin compared with benzylpenicillin. These characteristics indicate that NTP1 plasmid-coded beta-lactamase is very similar or identical to the "TEM-type" beta-lactamase, which is the most common beta-lactamase coded by R-plasmids in enteric bacteria. In minicells containing NTP1 plasmids, at least six plasmid-specific proteins were synthesized, and beta-lactamase was synthesized in a greater amount than other plasmid-coded proteins. In a cell-free transcription-translation coupled system from E. coli, NTP1 plasmid deoxyribonucleic acid directed the synthesis of several species of plasmid-specific proteins, including active beta-lactamase. The in vitro system also showed preferential synthesis of beta-lactamase, as was observed in minicells containing NTP1 plasmids.
机译：纯化了由小的非转移性R质粒NTP1编码的β-内酰胺酶，该酶赋予氨苄青霉素对其宿主细菌的抗性。发现NTP1质粒编码的β-内酰胺酶位于宿主大肠杆菌细胞的周质中，具有约25,000的分子量，并且与苄青霉素相比，对奥沙西林和甲氧西林显示相对较低的活性。这些特征表明，NTP1质粒编码的β-内酰胺酶与“ TEM型”β-内酰胺酶非常相似或相同，后者是肠细菌中R-质粒编码的最常见的β-内酰胺酶。在含有NTP1质粒的小细胞中，至少合成了六个质粒特异性蛋白，并且合成的β-内酰胺酶的数量比其他质粒编码的蛋白还要多。在来自大肠杆菌的无细胞转录-翻译偶联系统中，NTP1质粒脱氧核糖核酸指导几种质粒特异性蛋白质的合成，包括活性β-内酰胺酶。体外系统还显示优先合成β-内酰胺酶，正如在含有NTP1质粒的小细胞中观察到的那样。

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