Mutants defective in the energy-conserving NADH dehydrogenase of Salmonella typhimurium identified by a decrease in energy-dependent proteolysis after carbon starvation.
Mutants defective in the energy-conserving NADH dehydrogenase of Salmonella typhimurium identified by a decrease in energy-dependent proteolysis after carbon starvation.
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鼠伤寒沙门氏菌的能量守恒 NADH 脱氢酶有缺陷，通过碳饥饿后能量依赖性蛋白水解的减少来鉴定。
DOI：
10.1073/pnas.90.21.9877
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发表时间：
1993
影响因子：
11.1
通讯作者：
Elliott,T
中科院分区：
文献类型：
--
作者：
Archer,CD;Wang,X;Elliott,T
NADH脱氢酶是呼吸链的第一个组成部分。它将电子从NADH转移到泛醌，并同时建立跨膜的质子动力。在筛选具有来自hemA-lacZ蛋白融合的β-半乳糖苷酶表达增加的菌株时，分离出这种酶缺陷的鼠伤寒沙门氏菌突变体。这种意想不到的表型的结果，从稳定的杂交蛋白在碳饥饿，显然是由于蛋白水解攻击的能量需求。从一个插入突变体克隆的DNA片段的序列分析表明，S。鼠伤寒沙门氏菌有一个大的基因簇，编码能量保存的NADH脱氢酶，类似于最近在Paracoccus pesticans中描述的一个。这些发现建立了一个复杂的酶的功能，特别是在质子流出，是知之甚少的遗传分析的潜力。
NADH dehydrogenase is the first component of the respiratory chain. It transfers electrons from NADH to ubiquinone and concomitantly establishes a proton motive force across the membrane. Salmonella typhimurium mutants defective in this enzyme were isolated in a screen for strains with increased expression of beta-galactosidase from a hemA-lacZ protein fusion. This unexpected phenotype results from stabilization of the hybrid protein during carbon starvation and is apparently due to an energy requirement for proteolytic attack. Sequence analysis of DNA fragments cloned from an insertion mutant indicates that S. typhimurium has a large cluster of genes encoding the energy-conserving NADH dehydrogenase, similar to one recently described in Paracoccus denitrificans. These findings establish the potential for genetic analysis of a complex enzyme whose function, especially in proton efflux, is poorly understood.