[27] Thioredoxin genetics

Russel, Marjorie

doi:10.1016/0076-6879(95)52029-5

Cited by 17 publications

(16 citation statements)

References 40 publications

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“…Biogenesis of c-type cytochromes in a dsbD mutant is restored by addition of reducing agents (34), leading to the hypothesis that DsbD is involved in maintaining the cysteines in the heme binding site of the apo-cytochrome reduced, allowing the heme moiety to be attached. Thioredoxin is a highly abundant cytoplasmic protein which is involved in the reduction of certain cytoplasmic enzymes, including methionine sulfoxide reductase and ribonucleotide reductase (16,32). Mutants lacking either thioredoxin or DsbD display certain phenotypes similar to those observed in a dsbC mutant, supporting the proposal that they are required for DsbC to function properly (31).…”

mentioning

confidence: 60%

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin

et al. 1997

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The Escherichia coli periplasmic protein DsbC is active both in vivo and in vitro as a protein disulfide isomerase. For DsbC to attack incorrectly formed disulfide bonds in substrate proteins, its two active-site cysteines should be in the reduced form. Here we present evidence that, in wild-type cells, these two cysteines are reduced. Further, we show that a pathway involving the cytoplasmic proteins thioredoxin reductase and thioredoxin and the cytoplasmic membrane protein DsbD is responsible for the reduction of these cysteines. Thus, reducing potential is passed from cytoplasmic electron donors through the cytoplasmic membrane to DsbC. This pathway does not appear to utilize the cytoplasmic glutathione-glutaredoxin pathway. The redox state of the active-site cysteines of DsbC correlates quite closely with its ability to assist in the folding of proteins with multiple disulfide bonds. Analysis of the activity of mutant forms of DsbC in which either or both of these cysteines have been altered further supports the role of DsbC as a disulfide bond isomerase.

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confidence: 60%

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin

et al. 1997

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“…In most cases, their association with, and regulatory e ect on respective signaling molecules is neutralized. These redox responsive proteins include thioredoxin (reviewed by Russel, 1995) and glutathione S-transferase (GST ;Tew 1994;Hayes and Pulford, 1995). This review summarizes the current knowledge of ROS e ects on stress responsive proteins and highlights present understanding of possible underlying mechanisms.…”

Section: Introductionmentioning

confidence: 99%

Role of redox potential and reactive oxygen species in stress signaling

et al. 1999

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Stress-activated signaling cascades are a ected by altered redox potential. Key contributors to altered redox potential are reactive oxygen species (ROS) which are formed, in most cases, by exogenous genotoxic agents including irradiation, in¯ammatory cytokines and chemical carcinogens. ROS and altered redox potential can be considered as the primary intracellular changes which regulate protein kinases, thereby serving as an important cellular component linking external stimuli with signal transduction in stress response. The mechanisms, which underlie the ROS-mediated response, involve direct alteration of kinases and transcription factors, and indirect modulation of cysteine-rich redox-sensitive proteins exempli®ed by thioredoxin and glutathione Stransferase. This review summarizes the current understanding of the mechanisms contributing to ROS-related changes in key stress activated signaling cascades.

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“…However, it would be premature to rule out the existence of a redox gradient actively maintained by the cell among the cytoplasm, periplasm, and medium. At least, it seems that in the cytoplasm a reducing balance is established with three glutaredoxin activities (2), as well as the thioredoxin and thioredoxin reductase system (71).…”

Section: Why Disulfide Bonds and Where? Oxidation Of Transported Protmentioning

confidence: 99%