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Journal ArticleDOI

Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system.

Aristi P. Fernandes, +1 more
- 05 Jul 2004 - 
- Vol. 6, Iss: 1, pp 63-74
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TLDR
Glutaredoxins uniquely reduce mixed disulfides with glutathione via a monothiol mechanism where only an N-terminal low pKa Cys residue is required, by using their glutathionylation site.
Abstract
Most cells contain high levels of glutathione and multiple glutaredoxins, which utilize the reducing power of glutathione to catalyze disulfide reductions in the presence of NADPH and glutathione reductase (the glutaredoxin system). Glutaredoxins, like thioredoxins, may operate as dithiol reductants and are involved as alternative pathways in cellular functions such as formation of deoxyribonucleotides for DNA synthesis (by reducing the essential enzyme ribonucleotide reductase), the generation of reduced sulfur (via 3′-phosphoadenylylsulfate reductase), signal transduction, and the defense against oxidative stress. The three dithiol glutaredoxins of E. coli with the active-site sequence CPYC and a glutathione binding site in a thioredoxin/glutaredoxin fold display surprisingly different properties. These include the inducible OxyR-regulated 10-kDa Grx1 or the highly abundant 24-kDa glutathione S-transferase-like Grx2 (with Grx3 it accounts for 1% of total protein). Glutaredoxins uniquely reduce mixed dis...

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Citations
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Journal ArticleDOI

The thioredoxin antioxidant system.

TL;DR: The absence of a GSH-Grx system in some pathogenic bacteria such as Helicobacter pylori, Mycobacterium tuberculosis, and Staphylococcus aureus makes the bacterial Trx system essential for survival under oxidative stress, and provides an opportunity to kill these bacteria by targeting the TrxR-Trx system.
Journal ArticleDOI

Mitochondrial metabolism of reactive oxygen species.

TL;DR: It is suggested that mitochondria augment intracellular oxidative stress due primarily to failure of their ROS removal systems, whereas the role of mitochondrial ROS emission is yet to be determined and a net increase in mitochondrial ROS production in situ remains to be demonstrated.
Journal ArticleDOI

Antioxidant responses and cellular adjustments to oxidative stress.

TL;DR: The role of crucial cellular nucleophiles, such as glutathione, and their capacity to interact with oxidants and to establish networks with other critical enzymes such as peroxiredoxins are focused on.
Journal ArticleDOI

Real-time imaging of the intracellular glutathione redox potential.

TL;DR: It is demonstrated that the fusion of human glutaredoxin-1 to roGFP2 facilitates specific real-time equilibration between the sensor protein and the glutathione redox couple, which facilitated the observation of redox changes associated with growth factor availability, cell density, mitochondrial depolarization, respiratory burst activity and immune receptor stimulation.
Journal ArticleDOI

Redox-based regulation of signal transduction : Principles, pitfalls, and promises

TL;DR: Some of the recent findings that illuminate the significance of redox signaling and exciting future perspectives are reviewed to highlight some of the current pitfalls and the approaches needed to advance this important area of biochemical and biomedical research.
References
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Journal ArticleDOI

MOLMOL: a program for display and analysis of macromolecular structures.

TL;DR: Special efforts were made to allow for appropriate display and analysis of the sets of typically 20-40 conformers that are conventionally used to represent the result of an NMR structure determination, using functions for superimposing sets of conformers, calculation of root mean square distance (RMSD) values, identification of hydrogen bonds, and identification and listing of short distances between pairs of hydrogen atoms.
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The complete genome sequence of the Gram-positive bacterium Bacillus subtilis

F. Kunst, +154 more
- 20 Nov 1997 - 
TL;DR: Bacillus subtilis is the best-characterized member of the Gram-positive bacteria, indicating that bacteriophage infection has played an important evolutionary role in horizontal gene transfer, in particular in the propagation of bacterial pathogenesis.
Journal ArticleDOI

Oxidative Stress, Caloric Restriction, and Aging

TL;DR: Support for this hypothesis includes the following observations: (i) Overexpression of antioxidative enzymes retards the age-related accrual of oxidative damage and extends the maximum life-span of transgenic Drosophila melanogaster and (ii) Variations in longevity among different species inversely correlate with the rates of mitochondrial generation of the superoxide anion radical and hydrogen peroxide.
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Essential Bacillus subtilis genes

Kazuto Kobayashi, +98 more
TL;DR: To estimate the minimal gene set required to sustain bacterial life in nutritious conditions, a systematic inactivation of Bacillus subtilis genes was carried out and most genes involved in the Embden–Meyerhof–Parnas pathway are essential.
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