编码大肠杆菌不耐热毒素的顺反子。
Cistrons encoding Escherichia coli heat-labile toxin.
作者信息
Dallas W S, Gill D M, Falkow S
出版信息
J Bacteriol. 1979 Sep;139(3):850-8. doi: 10.1128/jb.139.3.850-858.1979.
Abstract
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.
摘要
对编码大肠杆菌不耐热毒素（LT）的两个顺反子的结构和产物进行了研究。LT脱氧核糖核酸（DNA）区域已作为质粒P307的DNA片段的一部分被分离出来，并且该片段与克隆载体pBR313连接。将各种长度的缺失突变引入LT DNA区域和相邻的DNA序列中。缺失分析表明，LT DNA区域的最大大小为1.2×10⁶道尔顿。已证明LT DNA区域编码两种蛋白质，分子量分别为11,500道尔顿和25,500道尔顿。对这些LT基因产物的功能进行了研究。11,500道尔顿的蛋白质对Y-1肾上腺细胞具有吸附活性，并且该蛋白质显示形成四个或五个单体的聚集体。25,500道尔顿的蛋白质显示具有腺苷酸环化酶激活活性。编码每种LT蛋白质的两个顺反子已定位在LT DNA区域的遗传图谱上。两个顺反子可能都从同一个启动子转录。
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