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首页> 外文期刊>Journal of bacteriology >Cistrons encoding Escherichia coli heat-labile toxin.
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Cistrons encoding Escherichia coli heat-labile toxin.

机译：Cistrons编码大肠杆菌热不稳定毒素。

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摘要

The structure and products of the two cistrons encoding the Escherichia coli heat-labile toxin (LT) were studied. The LT deoxyribonucleic acid (DNA) region had been isolated as part of a DNA fragment from the plasmid P307, and this fragment was joined to the cloning vector pBR313. Deletion mutations of various lengths were introduced into the LT DNA region and into the adjacent DNA sequences. Analysis of the deletions indicated that the maximum size of the LT DNA region was 1.2 x 10(6) daltons. Two proteins of 11,500 daltons and 25,500 daltons had been shown to be encoded by the LT DNA region. The functions of these LT gene products were investigated. The 11,500-dalton protein had an adsorption activity for Y-1 adrenal cells, and this protein was shown to form aggregates of four or five monomers. The 25,500-dalton protein was shown to have an adenylate cyclase-activating activity. The two cistrons encoding for each of the LT proteins have been located on a genetic map of the LT DNA region. Both cistrons are probably transcribed from the same promoter.
机译：研究了编码大肠杆菌大肠杆菌热不稳定毒素（LT）的两个轮廓的结构和产品。 LT脱氧核糖核酸（DNA）区域被分离为来自质粒P307的DNA片段的一部分，并且该片段连接到克隆载体PBR313。将各种长度的删除突变引入LT DNA区域并进入相邻的DNA序列。缺失分析表明，LT DNA区域的最大尺寸为1.2×10（6）道尔顿。已经显示出11,500道尔顿和25,500道尔顿的两种蛋白质被LT DNA区域编码。研究了这些LT基因产物的功能。 11,500-Dalton蛋白对Y-1肾上腺细胞具有吸附活性，并且显示该蛋白质形成四种或五种单体的聚集体。显示25,500-道尔顿蛋白质具有腺苷酸环酶活性活性。对LT蛋白的两个传感器已经位于LT DNA区域的遗传图上。两个轮胎可能从同一个启动子转录。

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