Geiser M, Schweitzer S, Grimm C
Gene. 1986;48(1):109-18. doi: 10.1016/0378-1119(86)90357-4.
One of the genes for the entomophatogenic crystal protein of Bacillus thuringiensis (subsp. kurstaki strain HD1) has been cloned in Escherichia coli, and its nucleotide sequence determined completely. The gene is contained within a 4360-bp-long HpaI-PstI DNA restriction fragment and codes for a polypeptide of 1,155 amino acid residues. The protoxin protein has a predicted Mr of 130,625. The E. coli-derived protoxin gene product is biologically active against Heliothis virescens larvae in a biotest assay. Extensive computer comparisons with other published B. thuringiensis subsp. kurstaki strains HD1, HD73, and B. thuringiensis subsp. sotto gene sequences reveal hypervariable regions in the first half of the protoxin coding sequence. These regions are responsible for the biological activity of the protein product of the cloned gene, and may explain the different biological activities of these different protoxins.
苏云金芽孢杆菌(库尔斯塔克亚种HD1菌株)的一种昆虫致病晶体蛋白基因已在大肠杆菌中克隆,并完全测定了其核苷酸序列。该基因包含在一个4360bp长的HpaI - PstI DNA限制性片段中,编码一个由1155个氨基酸残基组成的多肽。原毒素蛋白的预测分子量为130,625。在生物测试中,大肠杆菌衍生的原毒素基因产物对棉铃虫幼虫具有生物活性。与其他已发表的苏云金芽孢杆菌库尔斯塔克亚种HD1、HD73菌株以及苏云金芽孢杆菌 sotto亚种基因序列进行广泛的计算机比较,发现在原毒素编码序列的前半部分存在高变区。这些区域决定了克隆基因蛋白质产物的生物活性,并且可能解释了这些不同原毒素的不同生物活性。