78 research outputs found

    Crystal structure of a murine α-class glutathione S-transferase involved in cellular defense against oxidative stress

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    Glutathione S-transferases (GSTs) are ubiquitous multifunctional enzymes which play a key role in cellular detoxification. The enzymes protect the cells against toxicants by conjugating them to glutathione. Recently, a novel subgroup of α-class GSTs has been identified with altered substrate specificity which is particularly important for cellular defense against oxidative stress. Here, we report the crystal structure of murine GSTA4-4, which is the first structure of a prototypical member of this subgroup. The structure was solved by molecular replacement and refined to 2.9 Å resolution. It resembles the structure of other members of the GST superfamily, but reveals a distinct substrate binding site.

    cGAL, a temperature-robust GAL4–UAS system for Caenorhabditis elegans

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    The GAL4–UAS system is a powerful tool for manipulating gene expression, but its application in Caenorhabditis elegans has not been described. Here we systematically optimize the system's three main components to develop a temperature-optimized GAL4–UAS system (cGAL) that robustly controls gene expression in C. elegans from 15 to 25 °C. We demonstrate this system's utility in transcriptional reporter analysis, site-of-action experiments and exogenous transgene expression; and we provide a basic driver and effector toolkit

    Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress

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    Glutathione S-transferases (GSTs) are ubiquitous multifunctional enzymes which play a key role in cellular detoxification, The enzymes protect the cells against toxicants by conjugating them to glutathione, Recently, a novel subgroup of alpha-class GSTs has been identified with altered substrate specificity which is particularly important for cellular defense against oxidative stress, Here, me report the crystal structure of murine GSTA4-4, which is the first structure of a prototypical member of this subgroup, The structure was solved by molecular replacement and refined to 2.9 Angstrom resolution, It resembles the structure of other members of the GST superfamily, but reveals a distinct substrate binding site. (C) 1998 Federation of European Biochemical Societies
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