首页> 美国卫生研究院文献>Journal of Bacteriology >Increased ATP-dependent proteolytic activity in lon-deficient Escherichia coli strains lacking the DnaK protein.
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Increased ATP-dependent proteolytic activity in lon-deficient Escherichia coli strains lacking the DnaK protein.

机译:在缺乏DnaK蛋白的缺乏的大肠杆菌中ATP依赖的蛋白水解活性增加。

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摘要

Extracts made from Escherichia coli null dnaK strains contained elevated levels of ATP-dependent proteolytic activity compared with levels in extracts made from dnaK+ strains. This ATP-dependent proteolytic activity was not due to Lon, Clp, or Alp-associated protease. Comparison of the levels of ATP-dependent proteolytic activity present in lon rpoH dnaK mutants and in lon rpoH dnaK+ mutants showed that the level of ATP-dependent proteolytic activity was elevated in the lon rpoH dnaK mutant strain. These findings suggest that DnaK negatively regulates a new ATP-dependent proteolytic activity, independently of sigma 32. Other results indicate that an ATP-dependent proteolytic activity was increased in a lon alp strain after heat shock. It is not yet known whether the same protease is associated with the increased ATP-dependent proteolytic activity in the dnaK mutants and in the heat-shocked lon alph strain.
机译:与由dnaK +菌株制成的提取物中的水平相比,由大肠杆菌无效dnaK菌株制成的提取物包含更高水平的ATP依赖性蛋白水解活性。这种ATP依赖的蛋白水解活性不是由于Lon,Clp或Alp相关的蛋白酶。比较lon rpoH dnaK突变体和lon rpoH dnaK +突变体中ATP依赖的蛋白水解活性的水平表明,lon rpoH dnaK突变体菌株中ATP依赖的蛋白水解活性的水平升高。这些发现表明,DnaK独立于sigma 32负调控新的ATP依赖性蛋白水解活性。其他结果表明,lon阿尔卑斯菌株中热休克后ATP依赖性蛋白水解活性增加。尚不相同的蛋白酶是否与dnaK突变体和热休克的隆阿尔普菌株中增加的ATP依赖蛋白水解活性相关。

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