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Structural basis for yeast pathway in response to oxidative stress

  • Hefei National Laboratory for Physical Sciences at Microscale, and School of Life Sciences, University of Science and Technology of China, Hefei 230027, China

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  • Received Date: 28 June 2008
  • Rev Recd Date: 05 July 2008
  • Publish Date: 31 August 2008
    Abstract

  • Abstract

    The yeast Saccharomyces cerevisiae is a unicellular organism with the best research background. To date, there are 78 genes annotated to the term of response to oxidative stress in yeast. The encoded proteins of these genes could be classified into three groups, sensors, regulators and effectors. Taking advantage of the methodology of structural genomics, we started with all of the effectors and have solved all key effectors along the electron transfer pathway of thioredoxin and glutaredoxin systems. Moreover, a series of assays will be set up to identify the potential biochemical activities of the important effectors. Biochemical assays, in combination with protein-protein complex identification and structure solution, and the fast growing information in yeast databases, enable us to remodel a structure-based protein-protein interaction network of effectors in response to oxidative stress. These researches will provide us with some hints to design potential drugs for preventing oxidative stress-related diseases and aging.

    Abstract

    The yeast Saccharomyces cerevisiae is a unicellular organism with the best research background. To date, there are 78 genes annotated to the term of response to oxidative stress in yeast. The encoded proteins of these genes could be classified into three groups, sensors, regulators and effectors. Taking advantage of the methodology of structural genomics, we started with all of the effectors and have solved all key effectors along the electron transfer pathway of thioredoxin and glutaredoxin systems. Moreover, a series of assays will be set up to identify the potential biochemical activities of the important effectors. Biochemical assays, in combination with protein-protein complex identification and structure solution, and the fast growing information in yeast databases, enable us to remodel a structure-based protein-protein interaction network of effectors in response to oxidative stress. These researches will provide us with some hints to design potential drugs for preventing oxidative stress-related diseases and aging.
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    • References(26)
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    He W W, Wang Y, Liu W, et al. Crystal structure of Saccharomyces cerevisiae 6-phosphogluconate dehydrogenase Gnd1 [J]. BMC Struct Biol, 2007, 7:38.
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    Strand M K, Stuart G R, Longley M J, et al. POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase required for stability of mitochondrial DNA [J]. Eukaryot Cell, 2003, 2(4):809-820.
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    Kryukov G V, Kumar R A, Koc A, et al. Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase [J]. Proc Natl Acad Sci USA, 2002, 99(7):4 245-4 250.
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    Lillig C H, Holmgren A. Thioredoxin and related molecules： from biology to health and disease [J]. Antioxid Redox Signal, 2007, 9(1):25-47.
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    Bao R, Chen Y, Tang Y J, et al. Crystal structure of the yeast cytoplasmic thioredoxin Trx2 [J]. Proteins, 2007, 66(1): 246-249.
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    Weichsel A, Brailey J L, Montfort W R. Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin [J]. Biochem, 2007, 46: 219-227.
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    Sengupta R, Ryter S W, Zuckerbraun B S, et al. Thioredoxin catalyzes the denitrosation of low-molecular mass and protein S-nitrosothiols [J]. Biochem, 2007, 46: 8 472-8 483.
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    Salavej P, Spalteholz H, Arnhold J. Modification of amino acid residues in human serum albumin by myeloperoxidase [J]. Free Radic Biol Med, 2006,40:516-525.
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    Rhee S G, Chae H Z, Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling [J]. Free Radic Biol Med, 2005, 38(12):1 543-1 552.
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    Wood Z A, Schr der E, Robin Harris J, et al. Structure, mechanism and regulation of peroxiredoxins [J]. Trends Biochem Sci, 2003, 28(1):32-40.
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    Jang H H, Lee K O, Chi Y H, et al. Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function [J]. Cell, 2004, 117(5):625-635.
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    Park S G, Cha M K, Jeong W, et al. Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae [J]. J Biol Chem, 2000, 275(8):5 723-5 732.
    [21]
    Delaunay A, Pflieger D, Barrault M B, et al. A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation [J]. Cell, 2002, 111(4):471-481.
    [22]
    Grant C M. Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions [J]. Mol Microbiol, 2001, 39(3):533-541.
    [23]
    Yu J, Zhang N N, Yin P D, et al. Glutathionylation-triggered conformational changes of glutaredoxin Grx1 from the yeast Saccharomyces cerevisiae [J]. Proteins, 2008(in press).
    [24]
    Rodríguez-Manzaneque M T, Tamarit J, Bellí G, et al. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes [J]. Mol Biol Cell, 2002, 13(4):1 109-1 121.
    [25]
    Yu J, Zhou C Z. Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae [J]. Proteins, 2007, 68(4):972-979.
    [26]
    Yu J, Zhou C Z. Crystal structure of the dimeric Urm1 from the yeast Saccharomyces cerevisiae[J]. Proteins, 2008, 71(2):1 050-1 055.
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    [1]
    Marx J L. Oxygen free radicals linked to many diseases [J]. Science, 1985, 235: 529-531.
    [2]
    Wang M C, Bohmann D, Jasper H. JNK signaling confers tolerance to oxidative stress and extends lifespan in Drosophila [J]. Dev Cell, 2003, 5: 811-816.
    [3]
    Fabrizio P, Pozza F, Pletcher S D, et al. Regulation of longevity and stress resistance by Sch9 in yeast [J]. Science, 2001, 292: 288-290.
    [4]
    Veal E A, Ross S J, Malakasi P, et al. Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor [J]. J Biol Chem, 2003, 278(33): 30 896-30 904.
    [5]
    Okazaki S, Tachibana T, Naganuma A, et al. Multistep disulfide bond formation in Yap1 is required for sensing and transduction of H2O2 stress signal [J]. Mol Cell, 2007, 27(4):675-688.
    [6]
    He W W, Wang Y, Liu W, et al. Crystal structure of Saccharomyces cerevisiae 6-phosphogluconate dehydrogenase Gnd1 [J]. BMC Struct Biol, 2007, 7:38.
    [7]
    Strand M K, Stuart G R, Longley M J, et al. POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase required for stability of mitochondrial DNA [J]. Eukaryot Cell, 2003, 2(4):809-820.
    [8]
    Kryukov G V, Kumar R A, Koc A, et al. Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase [J]. Proc Natl Acad Sci USA, 2002, 99(7):4 245-4 250.
    [9]
    Trotter E W, Grant C M. Overlapping roles of the cytoplasmic and mitochondrial redox regulatory systems in the yeast Saccharomyces cerevisiae[J]. Eukaryot Cell, 2005, 4(2), 392-400.
    [10]
    Draculic T, Dawes I W, Grant C M. A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae [J]. Mol Microbiol, 2000, 36(5):1 167-1 174.
    [11]
    Pedrajas J R, Kosmidou E, Miranda-Vizuete A, et al. Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae [J]. J Biol Chem, 1999, 274(10):6 366-6 373.
    [12]
    Lillig C H, Holmgren A. Thioredoxin and related molecules： from biology to health and disease [J]. Antioxid Redox Signal, 2007, 9(1):25-47.
    [13]
    Bao R, Chen Y, Tang Y J, et al. Crystal structure of the yeast cytoplasmic thioredoxin Trx2 [J]. Proteins, 2007, 66(1): 246-249.
    [14]
    Weichsel A, Brailey J L, Montfort W R. Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin [J]. Biochem, 2007, 46: 219-227.
    [15]
    Sengupta R, Ryter S W, Zuckerbraun B S, et al. Thioredoxin catalyzes the denitrosation of low-molecular mass and protein S-nitrosothiols [J]. Biochem, 2007, 46: 8 472-8 483.
    [16]
    Salavej P, Spalteholz H, Arnhold J. Modification of amino acid residues in human serum albumin by myeloperoxidase [J]. Free Radic Biol Med, 2006,40:516-525.
    [17]
    Rhee S G, Chae H Z, Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling [J]. Free Radic Biol Med, 2005, 38(12):1 543-1 552.
    [18]
    Wood Z A, Schr der E, Robin Harris J, et al. Structure, mechanism and regulation of peroxiredoxins [J]. Trends Biochem Sci, 2003, 28(1):32-40.
    [19]
    Jang H H, Lee K O, Chi Y H, et al. Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function [J]. Cell, 2004, 117(5):625-635.
    [20]
    Park S G, Cha M K, Jeong W, et al. Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae [J]. J Biol Chem, 2000, 275(8):5 723-5 732.
    [21]
    Delaunay A, Pflieger D, Barrault M B, et al. A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation [J]. Cell, 2002, 111(4):471-481.
    [22]
    Grant C M. Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions [J]. Mol Microbiol, 2001, 39(3):533-541.
    [23]
    Yu J, Zhang N N, Yin P D, et al. Glutathionylation-triggered conformational changes of glutaredoxin Grx1 from the yeast Saccharomyces cerevisiae [J]. Proteins, 2008(in press).
    [24]
    Rodríguez-Manzaneque M T, Tamarit J, Bellí G, et al. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes [J]. Mol Biol Cell, 2002, 13(4):1 109-1 121.
    [25]
    Yu J, Zhou C Z. Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae [J]. Proteins, 2007, 68(4):972-979.
    [26]
    Yu J, Zhou C Z. Crystal structure of the dimeric Urm1 from the yeast Saccharomyces cerevisiae[J]. Proteins, 2008, 71(2):1 050-1 055.
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