Hiromi Y, Okamoto H, Gehring W J, Hotta Y
Cell. 1986 Jan 31;44(2):293-301. doi: 10.1016/0092-8674(86)90763-4.
Two Drosophila mutants KM75 and HH5, which are mutated in the act88F actin gene specific for the indirect flight muscles (IFM), synthesize heat shock proteins (hsps) constitutively in a tissue-specific manner. We have introduced cloned mutant act88F genes into a strain containing the wild-type act88F allele by P-element-mediated transformation. Flies transformed with a 4.05 kb KM75 act88F gene fragment encoding the p42 actin variant express both p42 and hsps specifically in the IFM. Using normal/mutant chimeric genes, the mutation sites of KM75 and HH5 were mapped within the sequence encoding the last 72 amino acids of actin. An in vitro mutated gene encoding a protein that lacks the 72 carboxy-terminal amino acids also induces constitutive hsp synthesis.
两个果蝇突变体KM75和HH5，它们在间接飞行肌（IFM）特有的act88F肌动蛋白基因中发生了突变，以组织特异性方式组成型合成热休克蛋白（hsps）。我们通过P元素介导的转化，将克隆的突变act88F基因导入含有野生型act88F等位基因的菌株中。用编码p42肌动蛋白变体的4.05 kb KM75 act88F基因片段转化的果蝇，在IFM中特异性地表达p42和hsps。使用正常/突变嵌合基因，将KM75和HH5的突变位点定位在编码肌动蛋白最后72个氨基酸的序列内。一个编码缺少72个羧基末端氨基酸的蛋白质的体外突变基因也诱导组成型hsp合成。
