The DnaK chaperone is necessary for α-complementation of β-galactosidase in Escherichia coli
The DnaK chaperone is necessary for α-complementation of β-galactosidase in Escherichia coli
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DOI：
10.1128/jb.184.24.7047-7054.2002
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发表时间：
2002-12-01
影响因子：
3.2
通讯作者：
Alix, JH
中科院分区：
文献类型：
--
作者：
Ferreira, NL;Alix, JH
我们在这里显示的参与分子伴侣DnaK从大肠杆菌在体内α-互补的P-半乳糖苷酶。在dnaK 756（Ts）突变体中，当生物体在30 ℃下生长时发生α-互补，但在37或40 ℃下则不会，尽管这些温度允许细菌生长。野生型dnaK的质粒驱动表达恢复了突变体中的et-互补，但也刺激了dnaK（+）菌株中的et-互补。在含有破坏的dnaK基因的突变体中（DeltadnaK 52：：Cm-r α-互补也受损，即使在30 ℃下也是如此。这一观察结果提供了一种简单和原始的表型，以检测蛋白质如DnaK 756分子伴侣在生理相关温度内的细微功能变化。
We show here the involvement of the molecular chaperone DnaK from Escherichia coli in the in vivo alpha-complementation of the P-galactosidase. In the dnaK756(Ts) mutant, alpha-complementation occurs when the organisms are grown at 30degreesC but not at 37 or 40degreesC, although these temperatures are permissive for bacterial growth. Plasmid-driven expression of wild-type dnaK restores the et-complementation in the mutant but also stimulates it in a dnaK(+) strain. In a mutant which contains a disrupted dnaK gene (DeltadnaK52::Cm-r alpha-complementation is also impaired, even at 30degreesC. This observation provides an easy and original phenotype to detect subtle functional changes in a protein such as the DnaK756 chaperone, within the physiologically relevant temperature.