cDNA Sequence and mRNA Expression of a Putative Glutathione S-Transferase from the Mole Cricket, Gryllotalpa orientalis

  • Kim, Iksoo (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technology) ;
  • Lee, Kwang-Sik (College of Natural Resources and Life Science, Dong-A University) ;
  • Jin, Byung-Rae (College of Natural Resources and Life Science, Dong-A University) ;
  • Kim, Jin-Won (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technology) ;
  • Ryu, Kang-Sun (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technology) ;
  • Ahn, Mi-Young (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technology)
  • Published : 2003.06.01

Abstract

The glutathione S-transferase (GSTs) are enzymes responsible for the protection of cells from chemical toxicants and oxidative stress. We describe here the cDNA sequence and mRNA expression of a putative GST from the mole cricket, Gryllotalpa orientalis. The G. orientalis GST cDNA sequences comprised of 621 bp encoding 207 amino acid residues. The multiple sequence alignment of G. orientalis GST gene with other known insect GSTs showed several conserved residues that may be essential for the enzymatic activity of the protein. Phylogenetic analysis of the deduced amino acid sequences of G. orientalis GST gene with other insect GST sequences revealed that the G. orientalis GST gene belongs to class I GST, forming a strong monophyletic group (100% bootstrap value) exclusively for class I GSTs from a diverse insect species. Northern blot analysis confirmed midgut-specific expression at transcriptional level, evidencing the midgut as a site for GST synthesis.

Keywords

References

  1. Armstrong, R. N. (1991) GIutathione S-transferases: reaction mechanism, structure, and function. Chem. Res. Toxicol. 4, 131-140 https://doi.org/10.1021/tx00020a001
  2. Arruda, L. K., L. D. Vailes, T. A. E, Platts-Mills, M. L. Hayden and M. D. Chapman (1997) Induction of IgE antibody responses by glutathione S-transferase from the German cockroach (Blattella germanica). J. BioI. Chem. 272, 20907-20912 https://doi.org/10.1074/jbc.272.33.20907
  3. Beall, C., C. Fyrberg, S. Song and E. Fryberg (1992) Isolation of a Drosophila gene encoding glutathione S-transferase. Biochem. Genet. 30, 515-527 https://doi.org/10.1007/BF01037590
  4. Chien, C. and W. C. Dauterman (1991) Studies on glutathione S-transferase in Helicoverpa (=Hetiothis) zea. Insect Biochem. 21, 857-864 https://doi.org/10.1016/0020-1790(91)90092-S
  5. Clark, A. G. (1989) The comparative enzymology of the gIutathione S-transferases from non-vertebrate organisms. Comp. Biochem. Physiol. 92B, 419-446
  6. Daniel, V. (1993) Glutathione S-transferases: gene structure and regulation of expression. Crit. Rev. Biochem. Molec. Biol. 28, 173-207 https://doi.org/10.3109/10409239309086794
  7. Feng, Q. L., K. G. Davey, A. S. D. Pang, M. Primavera, T. R. Ladd, S. C. Zheng, S. S. Sohi, A. Retnakaran and S. R. Palli (1999) Glutathione S-transferase from the spruce budworm, Choristoneura fumiferana: identification, characterization, localization, cDNA cloning, and expression, Insect Biochem. Mol. Biol. 29, 779-793 https://doi.org/10.1016/S0965-1748(99)00048-X
  8. Fouruier, D., J. M. Bride, M. Poirie, J. M. Berge and F. W. Plapp Jr (1992) Insect glutathione S-transferases: Biochemical characteristics of the major forms from houseflies susceptible and resistant to insecticides. J. BioI. Chem. 267, 1840-1845
  9. Franciosa, H. and J. B. Berge (1995) Glutathione S-transferase in house fly (Musca domesticd): Location of GST-l and GST-2 families, Insect Biochem. MoI. BioI. 25, 311-317 https://doi.org/10.1016/0965-1748(94)00053-K
  10. Grant, D. F. and F. Matsumura (1989) Glutathione S-trans-ferase 1 and 2 in susceptible and insecticide resistant Aedes aegypti. Pest. Biochem. Physiol. 33, 132-143 https://doi.org/10.1016/0048-3575(89)90004-7
  11. Garnier, J., D. J. Osguthorpe and B. Robson (1978) Analysis of the accuracy and implications of simple methods for Predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120 https://doi.org/10.1016/0022-2836(78)90297-8
  12. Huang, H. S., N. T. Hu, Y. E. Yao, C. Y. Wu, S. W. Chiang and C. N. Sun (1998) Molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the diamondback moth, PIutelIa Xylostella. Insect Biochem. Molec. Biol. 28, 651-658 https://doi.org/10.1016/S0965-1748(98)00049-6
  13. Ji, X., P. Zhang, R. N. Armstrong and G. L. Gilliland (1992) The three-dimensional structure of a glutathione S-transferases from the mu gene class. Structural analysis of the binary complex of isozyme 3-3 and glutathione at 2.2-A resolution. Biochem. 31, 10169-10183 https://doi.org/10.1021/bi00157a004
  14. Ji, X., E. C. von Rosenvinge, W. W. Johnson, S. I. Tomarew, J. Piatigorsky, R. N. Armstrong and G. L. Gilliland (1995) Three-dimensional structure, catalytic properties, and evolution, a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochem. 34, 5317-5328 https://doi.org/10.1021/bi00016a003
  15. Kim, I., K. S. Lee, B. R. Jin, E. S. Kim, H. S. Lee, M. Y. Ahn, H. D. Sohn and K. S. Ryu (2002) Molecular cloning of the Sec61p \gamma subunit homologue gene from the mole cricket, Gryllotnlpa orientalis. Int. J. Indust. Entomol. 5, 73-77
  16. Kim, I., K. S. Lee, K. S. Ryu, J. W. Kim, M. Y. Ahn, H. S. Lee, H. D. Sohn and B. R. Jin (2003) Molecular cloning and expression of a cDNA encoding putative chemosensory Protein from the mole cricket, Gryllotalpa orientalis. Int. J. Indust. Entomol. 6, 87-92
  17. Listowsky, I., M. Abramovitz, H. Homma and Y. Niitsu (1988) Intracellular binding and transport of hormones and xenobiotics by glutathione S-transferases. Drug Metahol. Rev. 19, 305-318 https://doi.org/10.3109/03602538808994138
  18. McMaster, G. K. and G. G. Carmichael (1977) Analysis of single- and double-stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridine orange. Proc. NatI. Acad. Sci. USA 74, 4835-4838 https://doi.org/10.1073/pnas.74.11.4835
  19. Motoyama, N. and W. C. Dauterman (1980) Glutathione Stransferases: their role in the metabolism of organophosphorus insecticides. Rev. Biochem. Toxic. 2, 49-69
  20. Nevo, E., A. Beiles, A. B. Korol, Y. I. Robin, T. Pavlicek and W. Hamilton (2000) Extraordinary multilocus genetic organization in mole cricket, Gryllotalpidae. Intl. Organic Evol. 54, 586-605 https://doi.org/10.1111/j.0014-3820.2000.tb00061.x
  21. Pickett, C. B. and A. Y. H. Lu (1989) Glutathione S-transferases: Gene structure, regulation, and biological function. Ann. Rev. Biochem. 58, 743-764 https://doi.org/10.1146/annurev.bi.58.070189.003523
  22. Prapanthadara, L., H. Ranson, P. Somboon and J. Hemingway (1998) Cloning, expression and characterization of an insect class I glutathione S-transferase from Anophetes dirus species B. Insect Biochem. Molec. Biol. 28, 321-329 https://doi.org/10.1016/S0965-1748(98)00006-X
  23. Ranson, H., F. Collins and J. Hemingway (1998) The role of alternative mRNA splicing in generating heterogeneity within the Anopheles gambiae class I glutathione S-transferase family. Proc. NatI. Acad. Sci. USA 95, 14284-14289 https://doi.org/10.1073/pnas.95.24.14284
  24. Reinemer, P., H. W. Dirr, R. Ladenstein, J. Schaffer, 0. Gallay and R. Guber (1991) The three-dimensional structure of class pi glutathione S-transferase in complex with gIutathione sulfonate at 2,3 A resolution. EMBO J. 10, 1997-2005
  25. Riskallah, M. R., W. C. Dauterman and E. Hodgson (1986) Nutritional effects on the induction of cytochrome \rho-450 and alutathione S-transferase in larvae of the tobacco budworm, Heliothis virescens (F.). Insect Biochem. 16, 491-499 https://doi.org/10.1016/0020-1790(86)90026-0
  26. Robertson, H. M., R. Martos, C. R. Sears, E. Z. Todres, K. K. Walden and J. B. Nardi (1999) Diversity of odourant binding proteins revealed by an expressed sequence tag project on male Manduca sexta moth antennae, Insect MoI. Biol. 8, 501-518 https://doi.org/10.1046/j.1365-2583.1999.00146.x
  27. Rushmore, T. H. and C. B. Pickett (1993) Glutathione S-transferases, structure, regulation, and therapeutic implications. J. Biol. Chem. 268, 11475-11478
  28. Salinas, A. E. and M. G. Wong (1999) Glutathione S-transferases a review. Curr. Med. Chem. 6, 279-309
  29. Snyder, M. J., J. K. Walding and R. Feyerreisen (1995) Glutathione S-transferases from larval Manduca sexta midgut: sequence of two cDNAs and enzyme induction, Insect Biochem. Molec. Biol. 25, 455-465 https://doi.org/10.1016/0965-1748(94)00083-B
  30. Swofford, D. L. (2000) PAUP*. Phylogenetic Analysis Using Parsimony (*and Other Methods), version 4. Sinauer Sunderland, MA (on disk)
  31. Tate, L. G., S. S. Nakat and E. Hodgson (1982) Comparison of detoxification activity in midgut and fat body during fifth instar development of the tobacco hornworm, Manduca sexta. Comp. Biochem. Physiol. 72C, 75-81
  32. Toung, Y. P. and C. P. Tu (1992) DrosophiIa glutathione S-transferases have sequence homology to stringent starvation protein of Escherichia coli. Biochem. Biophys. Res. Commun. 182, 355-360 https://doi.org/10.1016/S0006-291X(05)80152-4
  33. Toung, Y. P., T. S. Hsieh and C. P. Tu (1990) DrosophiIa gIutathione S-transferase 1-1 shares a region of sequence homology with the maize glutathione S-transferase III. Proc. NatI. Acad. Sci. USA 87, 31-35 https://doi.org/10.1073/pnas.87.1.31
  34. Vontas, J. G., G. J. Small, D. C. Nikou, H. Ranson and J. Hemingway (2002) Purification, molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the rice brown planthopper, Nilaparvata lugens. Biochem. J. 362, 329-337 https://doi.org/10.1042/0264-6021:3620329
  35. Wang, J. Y., S. McCommas and M. Syvanen (1991) Molecular cloning of a glutathione S-transferase overproduced in an insecticide-resistant strain of the housefly (Musca domestica). MoI. Gen. Genet. 121, 260-266
  36. Yu, S. J. (1982) Host plant induction of glulathione S-transferase in the fall armyworm. Pest. Biochem. Physiol. 18, 101-106 https://doi.org/10.1016/0048-3575(82)90092-X
  37. Yu, S. J. (1989) Purification and characterization of glutathione S-transferases from five phytophagous lepidoptera. Pest. Biochem. Physiol. 35, 97-105 https://doi.org/10.1016/0048-3575(89)90107-7