大肠杆菌中二硫键异构化的体内途径。
An in vivo pathway for disulfide bond isomerization in Escherichia coli.
作者信息
Rietsch A, Belin D, Martin N, Beckwith J
机构信息
Department of Microbilogy and Molecular Genetics, harvard Medical School, Boston, MA 02115, USA.
出版信息
Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):13048-53. doi: 10.1073/pnas.93.23.13048.
Abstract
Biochemical studies have shown that the periplasmic protein disulfide oxidoreductase DsbC can isomerize aberrant disulfide bonds. Here we present the first evidence for an in vivo role of DsbC in disulfide bond isomerization. Furthermore, our data suggest that the enzymes DsbA and DsbC play distinct roles in the cell in disulfide bond formation and isomerization, respectively. We have shown that mutants in dsbC display a defect in disulfide bond formation specific for proteins with multiple disulfide bonds. The defect can be complemented by the addition of reduced dithiothreitol to the medium, suggesting that absence of DsbC results in accumulation of misoxidized proteins. Mutations in the dipZ and trxA genes have similar phenotypes. We propose that DipZ, a cytoplasmic membrane protein with a thioredoxin-like domain, and thioredoxin, the product of the trxA gene, are components of a pathway for maintaining DsbC active as a protein disulfide bond isomerase.
摘要
生化研究表明，周质蛋白二硫键氧化还原酶DsbC能够使异常二硫键发生异构化。在此，我们首次提供了DsbC在体内二硫键异构化中发挥作用的证据。此外，我们的数据表明，酶DsbA和DsbC在细胞内分别在二硫键形成和异构化过程中发挥着不同的作用。我们已经表明，dsbC突变体在具有多个二硫键的蛋白质的二硫键形成方面表现出缺陷。通过向培养基中添加还原型二硫苏糖醇可以弥补该缺陷，这表明缺乏DsbC会导致错误氧化的蛋白质积累。dipZ和trxA基因的突变具有相似的表型。我们提出，具有硫氧还蛋白样结构域的细胞质膜蛋白DipZ以及trxA基因的产物硫氧还蛋白，是维持DsbC作为蛋白质二硫键异构酶活性的途径的组成部分。
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本文引用的文献
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A pathway for disulfide bond formation in vivo.体内二硫键形成的一条途径。
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A mutation blocking the formation of membrane or periplasmic endogenous and exogenous c-type cytochromes in Escherichia coli permits the cytoplasmic formation of Hydrogenobacter thermophilus holo cytochrome c552.在大肠杆菌中，一种阻止膜或周质中外源和内源c型细胞色素形成的突变，使得嗜热栖热菌全细胞色素c552能够在细胞质中形成。
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The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation.大肠杆菌dsbC（xprA）基因编码一种参与二硫键形成的周质蛋白。
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Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.菊花欧文氏菌和大肠杆菌周质蛋白DsbC的特性研究：具有二硫键异构酶活性
EMBO J. 1994 Apr 15;13(8):2007-12. doi: 10.1002/j.1460-2075.1994.tb06470.x.
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Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein.特定硫醇化合物可弥补携带膜结合二硫键异构酶样蛋白突变的大肠杆菌中c型细胞色素生物合成的缺陷。
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Proc Natl Acad Sci U S A. 1993 Aug 1;90(15):7084-8. doi: 10.1073/pnas.90.15.7084.
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Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli.大肠杆菌中一种新的二硫键异构酶样蛋白（DsbD）的鉴定与特性分析。
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The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain.大肠杆菌中c型细胞色素的生物合成需要一种膜结合蛋白DipZ，它具有一个类似蛋白质二硫键异构酶的结构域。
Mol Microbiol. 1995 Mar;15(6):1139-50. doi: 10.1111/j.1365-2958.1995.tb02287.x.
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Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12.大肠杆菌K-12中与铜耐受性相关的染色体位点的分子遗传学
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DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA.通过其活性位点半胱氨酸实现的DsbA与DsbB的相互作用。来自DsbA一个奇数半胱氨酸突变体的证据。
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