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首页> 外文期刊>Journal of Molecular Biology >Polarity Effects in the Lactose Operon of Escherichia coli.
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Polarity Effects in the Lactose Operon of Escherichia coli.

机译：大肠杆菌乳糖操纵子中的极性影响。

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摘要

An intergenic RNA segment between lacY and lacA of the lactose operon in Escherichia coli is cleaved by RNase P, an endoribonuclease. The cleavage of the intergenic RNA was ten times less efficient than cleavage of a tRNA precursor in vitro. Fragments of the RNase P cleavage product are detectable in vivo in the wild-type strain but not in a mutant strain at the restrictive temperature. The cleavage product that contains lacA in the wild-type strain was quickly degraded. When this intergenic segment was cloned upstream of a reporter gene, the expression of the reporter gene was also inhibited substantially in wild-type E.coli, but not in a temperature sensitive mutant strain in RNase P at the restrictive temperature. These results support data regarding the natural polarity between lacZ versus lacA, the downstream gene.
机译：大肠杆菌中乳糖操纵子的lacY和lacA之间的基因间RNA片段被核糖核酸内切酶RNase P切割。基因间RNA的切割效率比体外tRNA前体的切割效率低十倍。在限制性温度下，在野生型菌株中体内可检测到RNA酶P切割产物的片段，而在突变型菌株中则无法检测到。野生型菌株中包含lacA的切割产物迅速降解。当将此基因间片段克隆到报告基因的上游时，报告基因的表达在野生型大肠杆菌中也得到了显着抑制，但在限制性温度下在RNase P中的温度敏感突变株中没有受到抑制。这些结果支持有关lacZ与下游基因lacA之间的自然极性的数据。

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