大肠杆菌中三甲胺N-氧化物（TMAO）还原酶的调控：tor::Mud1操纵子融合分析
Regulation of the trimethylamine N-oxide (TMAO) reductase in Escherichia coli: analysis of tor::Mud1 operon fusion.
作者信息
Pascal M C, Burini J F, Chippaux M
出版信息
Mol Gen Genet. 1984;195(1-2):351-5. doi: 10.1007/BF00332770.
Mud1 insertion mutants of Escherichia coli were obtained in which the lac structural genes were fused to the promoter of torA, a gene encoding the trimethylamine N-oxide (TMAO) reductase. Expression of the fusion is induced by TMAO and repressed by oxygen. However, in contrast to the nar operon which codes for the nitrate reductase structural genes, the tor::Mud1 fusion was found to be independent of the positive control exerted by the nirR gene product and not repressed by the molybdenum cofactor. The torA gene which is strongly linked to pyrF (28.3U) is different from any tor gene already described in E. coli or in Salmonella typhimurium.
获得了大肠杆菌的Mud1插入突变体，其中乳糖操纵子结构基因与torA基因的启动子融合，torA基因编码三甲胺N-氧化物（TMAO）还原酶。融合基因的表达由TMAO诱导并受氧气抑制。然而，与编码硝酸还原酶结构基因的nar操纵子不同，发现tor::Mud1融合基因独立于nirR基因产物施加的正调控，并且不受钼辅因子的抑制。与pyrF紧密连锁（28.3U）的torA基因不同于大肠杆菌或鼠伤寒沙门氏菌中已描述的任何tor基因。
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