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Gene Review

GstS1  -  Glutathione S transferase S1

Drosophila melanogaster

Synonyms: CG8938, DmGST-2, DmGST2, DmGSTS1, DmGSTS1-1, ...
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Disease relevance of GstS1


High impact information on GstS1

  • Furthermore, overexpression of GstS1 in DA neurons suppresses neurodegeneration in parkin mutants [4].
  • Recombinant rArl1 fused to glutathione-S-transferase (GST) to create GST-rArl1 binds GTP-gamma-S in a dose-dependent manner [5].
  • We find that within the PTM region, the cysteine residues required for GST-type activity are unnecessary for invertebrate CLIC function, but that specific residues within the proposed transmembrane helix are necessary for correct targeting and protein function [6].
  • The GST-2 dimer shows the canonical GST fold with glutathione (GSH) ordered in only one of the two binding sites [7].
  • It was recently shown that GST-2 exhibits considerable conjugation activity for 4-hydroxynonenal (4-HNE), a lipid peroxidation product, raising the possibility that it has a major anti-oxidant role in the flight muscle [7].

Chemical compound and disease context of GstS1


Biological context of GstS1


Anatomical context of GstS1

  • This results in the release of GST-2 from the myofibril [13].
  • GST-2 is present in the asynchronous indirect flight muscles but not in the synchronous tergal depressor of the trochanter (jump muscle) [13].
  • Genetic dissection of the sarcomere showed that GST-2 is stably associated with the thin filaments but the presence of myosin is required to achieve the correct stoichiometry, suggesting that there is also an interaction with the thick filament [13].
  • By creating GST (glutathione S-transferase)-fused LG1, LG2, LG4 and LG5 proteins, we found that only LG4 is active for the adhesion of human HT1080 cells, human umbilical vein endothelial cells and Drosophila haemocytes Kc167 with a half-saturating concentration of 20 microg/ml [14].

Associations of GstS1 with chemical compounds

  • Drosophila strains carrying P-element insertions in the GstS1 gene have a reduced capacity for glutathione conjugation of 4-HNE [1].
  • These GSTs have poor activity with common GST substrates, but exhibit novel glutathione-dependent thioltransferase, dehydroascorbate reductase and monomethylarsonate reductase activities, and modulate Ca release by ryanodine receptors [15].
  • These results are in contrast to induction responses we observed for the natural plant compound caffeine and the barbituate drug phenobarbital, both of which highly induced a number of P450 and GST genes under the same short exposure regime [11].
  • DDT elicited the low-level induction of one GST and one P450 [11].
  • This sequence, when compared with that of subunit 12 recently published by Ogura, Nishiyama, Okada, Kajita, Narihata, Watabe, Hiratsuka & Watabe [(1991) Biochem. Biophys. Res. Commun. 181, 1294-1300] proves that Theta is a separate multigene class of GST with little amino acid sequence identity with Mu-, Alpha- or Pi-class enzymes [3].

Other interactions of GstS1

  • In conclusion, we have discovered a new catalytic activity for an Omega class GST and that CG6781 is the structural gene for sepia which encodes PDA synthase [16].
  • An N-terminal extension found in GST-2 is unique within the sigma GST class and may be involved in its interaction with Tn-H or modulate its enzymatic function [17].
  • Significant genotype--environment associations were found for five of the six loci, and after correcting for geographic location significant associations remained for Est-2 and Adh-1 gene frequencies and heterozygosities and for Pgm gene frequencies [18].

Analytical, diagnostic and therapeutic context of GstS1


  1. Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products. Singh, S.P., Coronella, J.A., Benes, H., Cochrane, B.J., Zimniak, P. Eur. J. Biochem. (2001) [Pubmed]
  2. Downregulation of CD4 by human immunodeficiency virus type 1 nef is dependent on clathrin and involves direct interaction of nef with the AP2 clathrin adaptor. Chaudhuri, R., Lindwasser, O.W., Smith, W.J., Hurley, J.H., Bonifacino, J.S. J. Virol. (2007) [Pubmed]
  3. An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences. Pemble, S.E., Taylor, J.B. Biochem. J. (1992) [Pubmed]
  4. Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease. Whitworth, A.J., Theodore, D.A., Greene, J.C., Benes, H., Wes, P.D., Pallanck, L.J. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  5. The mammalian ARF-like protein 1 (Arl1) is associated with the Golgi complex. Lowe, S.L., Wong, S.H., Hong, W. J. Cell. Sci. (1996) [Pubmed]
  6. Mapping functional domains of chloride intracellular channel (CLIC) proteins in vivo. Berry, K.L., Hobert, O. J. Mol. Biol. (2006) [Pubmed]
  7. Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products. Agianian, B., Tucker, P.A., Schouten, A., Leonard, K., Bullard, B., Gros, P. J. Mol. Biol. (2003) [Pubmed]
  8. Glutathione transferase gene family from the housefly Musca domestica. Syvanen, M., Zhou, Z.H., Wang, J.Y. Mol. Gen. Genet. (1994) [Pubmed]
  9. Isolation of a Drosophila gene encoding glutathione S-transferase. Beall, C., Fyrberg, C., Song, S., Fyrberg, E. Biochem. Genet. (1992) [Pubmed]
  10. The Suppressor of Killer of prune, a unique glutathione S-transferase. Provost, E., Shearn, A. J. Bioenerg. Biomembr. (2006) [Pubmed]
  11. A comparison of Drosophila melanogaster detoxification gene induction responses for six insecticides, caffeine and phenobarbital. Willoughby, L., Chung, H., Lumb, C., Robin, C., Batterham, P., Daborn, P.J. Insect Biochem. Mol. Biol. (2006) [Pubmed]
  12. Isolation and characterization of a cDNA clone coding for a glutathione S-transferase class delta enzyme from the biting midge Culicoides variipennis sonorensis Wirth and Jones. Abdallah, M.A., Pollenz, R.S., Droog, F.N., Nunamaker, R.A., Tabachnick, W.J., Murphy, K.E. Biochem. Genet. (2000) [Pubmed]
  13. Interaction of troponin-H and glutathione S-transferase-2 in the indirect flight muscles of Drosophila melanogaster. Clayton, J.D., Cripps, R.M., Sparrow, J.C., Bullard, B. J. Muscle Res. Cell. Motil. (1998) [Pubmed]
  14. Mammalian and Drosophila cells adhere to the laminin alpha4 LG4 domain through syndecans, but not glypicans. Yamashita, H., Goto, A., Kadowaki, T., Kitagawa, Y. Biochem. J. (2004) [Pubmed]
  15. Characterization of the human Omega class glutathione transferase genes and associated polymorphisms. Whitbread, A.K., Tetlow, N., Eyre, H.J., Sutherland, G.R., Board, P.G. Pharmacogenetics (2003) [Pubmed]
  16. Identification and characteristics of the structural gene for the Drosophila eye colour mutant sepia, encoding PDA synthase, a member of the Omega class glutathione S-transferases. Kim, J., Suh, H., Kim, S., Kim, K., Ahn, C., Yim, J. Biochem. J. (2006) [Pubmed]
  17. Crystallization and preliminary X-ray analysis of Drosophila glutathione S-transferase-2. Agianian, B., Clayton, J.D., Leonard, K., Tucker, P., Bullard, B., Gros, P. Acta Crystallogr. D Biol. Crystallogr. (2001) [Pubmed]
  18. Allozyme genotype--environment relationships in natural populations of Drosophila buzzatii. Mulley, J.C., James, J.W., Barker, J.S. Biochem. Genet. (1979) [Pubmed]
  19. Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptor. Cho, Y.S., Kim, E.J., Park, U.H., Sin, H.S., Um, S.J. J. Biol. Chem. (2006) [Pubmed]
  20. Functional expression of a Drosophila antifungal peptide in Escherichia coli. Yuan, Y., Gao, B., Zhu, S. Protein Expr. Purif. (2007) [Pubmed]
  21. Transcriptional activity of Sp1 is regulated by molecular interactions between the zinc finger DNA binding domain and the inhibitory domain with corepressors, and this interaction is modulated by MEK. Lee, J.A., Suh, D.C., Kang, J.E., Kim, M.H., Park, H., Lee, M.N., Kim, J.M., Jeon, B.N., Roh, H.E., Yu, M.Y., Choi, K.Y., Kim, K.Y., Hur, M.W. J. Biol. Chem. (2005) [Pubmed]
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