메뉴 건너뛰기




Volumn 38, Issue 12, 2008, Pages 1158-1164

Identification, genomic organization and expression pattern of glutathione S-transferase in the silkworm, Bombyx mori

Author keywords

Bombyx mori; Expression pattern; Genomic organization; Glutathione S transferases

Indexed keywords

GLUTATHIONE TRANSFERASE;

EID: 59649107036     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2008.08.002     Document Type: Article
Times cited : (129)

References (47)
  • 1
    • 0041917283 scopus 로고    scopus 로고
    • Ultrastructure of maxillary sensilla in the silkworm, Bombyx mori: differences among strains?
    • Akaoka K. Ultrastructure of maxillary sensilla in the silkworm, Bombyx mori: differences among strains?. J. Insect Biotech. Sericology 72 (2003) 117-125
    • (2003) J. Insect Biotech. Sericology , vol.72 , pp. 117-125
    • Akaoka, K.1
  • 3
    • 0031439569 scopus 로고    scopus 로고
    • Zeta, a novel class of glutathione transferases in a range of species from plants to humans
    • Board P.G., Baker R.T., Chelvanayagam G., and Jermiin L.S. Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem. J. 328 (1997) 929-935
    • (1997) Biochem. J. , vol.328 , pp. 929-935
    • Board, P.G.1    Baker, R.T.2    Chelvanayagam, G.3    Jermiin, L.S.4
  • 5
    • 0000104664 scopus 로고    scopus 로고
    • Fly fishing for GSTs: a unified nomenclature for mammalian and insect glutathione transferases
    • Chelvanayagam G., Parker M.W., and Board P.G. Fly fishing for GSTs: a unified nomenclature for mammalian and insect glutathione transferases. Chem. Biol. Interact. 133 (2001) 256-260
    • (2001) Chem. Biol. Interact. , vol.133 , pp. 256-260
    • Chelvanayagam, G.1    Parker, M.W.2    Board, P.G.3
  • 6
    • 0002746624 scopus 로고
    • Glutathione transferase isozymes of diamondback moth larvae and their role in the degradation of some organophosphorus insecticides
    • Chiang F.M., and Sun C.N. Glutathione transferase isozymes of diamondback moth larvae and their role in the degradation of some organophosphorus insecticides. Pestic. Biochem. Physiol. 45 (1993) 7-14
    • (1993) Pestic. Biochem. Physiol. , vol.45 , pp. 7-14
    • Chiang, F.M.1    Sun, C.N.2
  • 7
    • 0021738417 scopus 로고
    • Evidence that DDT-dehydrochlorinase from the house fly is a glutathione S-transferase
    • Clark A.G., and Shamaan N.A. Evidence that DDT-dehydrochlorinase from the house fly is a glutathione S-transferase. Pestic. Biochem. Physiol. 22 (1984) 249-261
    • (1984) Pestic. Biochem. Physiol. , vol.22 , pp. 249-261
    • Clark, A.G.1    Shamaan, N.A.2
  • 9
    • 9144243812 scopus 로고    scopus 로고
    • The Anopheles gambiae glutathione transferase supergene family: annotation, phylogeny and expression profiles
    • Ding Y., Ortelli F., Rossiter L.C., Hemingway J., and Ranson H. The Anopheles gambiae glutathione transferase supergene family: annotation, phylogeny and expression profiles. BMC Genomics 4 (2003) 35
    • (2003) BMC Genomics , vol.4 , pp. 35
    • Ding, Y.1    Ortelli, F.2    Rossiter, L.C.3    Hemingway, J.4    Ranson, H.5
  • 10
    • 0035313034 scopus 로고    scopus 로고
    • Why do genes have introns? Recombination might add a new piece to the puzzle
    • Duret L. Why do genes have introns? Recombination might add a new piece to the puzzle. Trends Genet. 17 (2001) 172-175
    • (2001) Trends Genet. , vol.17 , pp. 172-175
    • Duret, L.1
  • 11
    • 0003437299 scopus 로고    scopus 로고
    • Distributed by the author, Department of Genome Sciences, University of Washington, Seattle
    • Felsenstein J. PHYLIP (Phylogeny Inference Package) Version 3.65. Distributed by the author (2005), Department of Genome Sciences, University of Washington, Seattle
    • (2005) PHYLIP (Phylogeny Inference Package) Version 3.65
    • Felsenstein, J.1
  • 13
    • 25844481290 scopus 로고    scopus 로고
    • Patterns of intron sequence evolution in Drosophila are dependent upon length and GC content
    • Haddrill P.R., Charlesworth B., Halligan D.L., and Andolfatto P. Patterns of intron sequence evolution in Drosophila are dependent upon length and GC content. Genome Biol. 6 (2005) R67
    • (2005) Genome Biol. , vol.6
    • Haddrill, P.R.1    Charlesworth, B.2    Halligan, D.L.3    Andolfatto, P.4
  • 15
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J.D., and Pulford D.J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30 (1995) 445-600
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 16
    • 0032168783 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the diamondback moth, Plutella xylostella
    • Huang H.S., Hu N.T., Yao Y.E., Wu C.Y., Chiang S.W., and Sun C.N. Molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the diamondback moth, Plutella xylostella. Insect Biochem. Mol. Biol. 28 (1998) 651-658
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 651-658
    • Huang, H.S.1    Hu, N.T.2    Yao, Y.E.3    Wu, C.Y.4    Chiang, S.W.5    Sun, C.N.6
  • 17
    • 0033011878 scopus 로고    scopus 로고
    • Common structural features of MAPEG-a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism
    • Jakobsson P.J., Morgenstern R., Mancini J., Ford-Hutchinson A., and Persson B. Common structural features of MAPEG-a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Sci. 8 (1999) 689-692
    • (1999) Protein Sci. , vol.8 , pp. 689-692
    • Jakobsson, P.J.1    Morgenstern, R.2    Mancini, J.3    Ford-Hutchinson, A.4    Persson, B.5
  • 18
    • 0000646193 scopus 로고
    • Glutathione transferase isozymes involved in insecticide resistance of diamondback moth larvae
    • Ku C.C., Chiang F.M., Hsin C.Y., Yao Y.E., and Sun C.N. Glutathione transferase isozymes involved in insecticide resistance of diamondback moth larvae. Pestic. Biochem. Physiol. 50 (1994) 191-197
    • (1994) Pestic. Biochem. Physiol. , vol.50 , pp. 191-197
    • Ku, C.C.1    Chiang, F.M.2    Hsin, C.Y.3    Yao, Y.E.4    Sun, C.N.5
  • 20
    • 0345832239 scopus 로고    scopus 로고
    • Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class Kappa enzyme rGSTK1-1
    • Lander J.E., Parsons J.F., Rife C.L., Gilliland G.L., and Armstrong R.N. Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class Kappa enzyme rGSTK1-1. Biochemistry 43 (2004) 352-361
    • (2004) Biochemistry , vol.43 , pp. 352-361
    • Lander, J.E.1    Parsons, J.F.2    Rife, C.L.3    Gilliland, G.L.4    Armstrong, R.N.5
  • 21
    • 0003421005 scopus 로고    scopus 로고
    • Sinauer Associates, Sunderland, Massachusetts
    • Li W.H. Molecular Evolution (1997), Sinauer Associates, Sunderland, Massachusetts
    • (1997) Molecular Evolution
    • Li, W.H.1
  • 22
    • 33846401539 scopus 로고    scopus 로고
    • Molecular mechanisms of metabolic resistance to synthetic and natural xenobiotics
    • Li X., Schuler M.A., and Berenbaum M.R. Molecular mechanisms of metabolic resistance to synthetic and natural xenobiotics. Annu. Rev. Entomol. 52 (2006) 231-253
    • (2006) Annu. Rev. Entomol. , vol.52 , pp. 231-253
    • Li, X.1    Schuler, M.A.2    Berenbaum, M.R.3
  • 24
    • 1942533492 scopus 로고    scopus 로고
    • Gene and protein characterization of the human glutathione S-transferase kappa and evidence for a peroxisomal localization
    • Morel F., Rauch C., Petit E., Piton A., Theret N., Coles B., and Guillouzo A. Gene and protein characterization of the human glutathione S-transferase kappa and evidence for a peroxisomal localization. J. Biol. Chem. 279 (2004) 16246-16253
    • (2004) J. Biol. Chem. , vol.279 , pp. 16246-16253
    • Morel, F.1    Rauch, C.2    Petit, E.3    Piton, A.4    Theret, N.5    Coles, B.6    Guillouzo, A.7
  • 25
    • 0002431731 scopus 로고
    • Glutathione S-transferases: their role in the metabolism of organophosphorus insecticides
    • Motoyama N., and Dauterman W.C. Glutathione S-transferases: their role in the metabolism of organophosphorus insecticides. Rev. Biochem. Toxicol. 2 (1980) 49-69
    • (1980) Rev. Biochem. Toxicol. , vol.2 , pp. 49-69
    • Motoyama, N.1    Dauterman, W.C.2
  • 26
    • 0031106147 scopus 로고    scopus 로고
    • Changes in protein metabolism in hemolymph and fat body of the silkworm, Bombyx mori (Lepidoptera: Bombycidae), in response to organophosphorus insecticide toxicity
    • Nath B.S., Suresh A., Varma B.M., and Kumar R.P.S. Changes in protein metabolism in hemolymph and fat body of the silkworm, Bombyx mori (Lepidoptera: Bombycidae), in response to organophosphorus insecticide toxicity. Ecotoxicol. Environ. Saf. 36 (1997) 169-173
    • (1997) Ecotoxicol. Environ. Saf. , vol.36 , pp. 169-173
    • Nath, B.S.1    Suresh, A.2    Varma, B.M.3    Kumar, R.P.S.4
  • 27
    • 23844535912 scopus 로고    scopus 로고
    • Identification of cytochrome P450 and glutathione S-transferase genes preferentially expressed in chemosensory organs of the swallowtail butterfly, Papilio xuthus L.
    • Ono H., Ozaki K., and Yoshikawa H. Identification of cytochrome P450 and glutathione S-transferase genes preferentially expressed in chemosensory organs of the swallowtail butterfly, Papilio xuthus L. Insect Biochem. Mol. Biol. 35 (2005) 837-846
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 837-846
    • Ono, H.1    Ozaki, K.2    Yoshikawa, H.3
  • 28
    • 0035887445 scopus 로고    scopus 로고
    • Identification of a novel class of insect glutathione S-transferases involved in DDT resistance in the malaria vector, Anopheles gambiae
    • Ranson H., Rossiter L., Ortelli F., Jensen B., Wang X., Roth C.W., Collins F.H., and Hemingway J. Identification of a novel class of insect glutathione S-transferases involved in DDT resistance in the malaria vector, Anopheles gambiae. Biochem. J. 359 (2001) 295-304
    • (2001) Biochem. J. , vol.359 , pp. 295-304
    • Ranson, H.1    Rossiter, L.2    Ortelli, F.3    Jensen, B.4    Wang, X.5    Roth, C.W.6    Collins, F.H.7    Hemingway, J.8
  • 30
    • 0033153407 scopus 로고    scopus 로고
    • An olfactory-specific glutathione-S-transferase in the sphinx moth Manduca sexta
    • Rogers M.E., Jani M.K., and Vogt R. An olfactory-specific glutathione-S-transferase in the sphinx moth Manduca sexta. J. Exp. Biol. 202 (1999) 1625-1637
    • (1999) J. Exp. Biol. , vol.202 , pp. 1625-1637
    • Rogers, M.E.1    Jani, M.K.2    Vogt, R.3
  • 31
    • 0023375195 scopus 로고
    • The neighbour-joining method: a new method for constructing phylogenetic trees
    • Saitou N., and Nei M. The neighbour-joining method: a new method for constructing phylogenetic trees. Mol. Biol. Evol. 4 (1987) 406-425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 32
    • 0037337927 scopus 로고    scopus 로고
    • Cloning, expression and biochemical characterization of one Epsilon class (GST-3) and ten Delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the Epsilon class
    • Sawicki R., Singh S.P., Mondal A.K., Benes H., and Zimniak P. Cloning, expression and biochemical characterization of one Epsilon class (GST-3) and ten Delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the Epsilon class. Biochem. J. 370 (2003) 661-669
    • (2003) Biochem. J. , vol.370 , pp. 661-669
    • Sawicki, R.1    Singh, S.P.2    Mondal, A.K.3    Benes, H.4    Zimniak, P.5
  • 33
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan D., Meade G., Foley V.M., and Dowd C.A. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360 (2001) 1-16
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 34
    • 0034833919 scopus 로고    scopus 로고
    • 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., and Zimniak P. Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products. Eur. J. Biochem. 268 (2001) 2912-2923
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2912-2923
    • Singh, S.P.1    Coronella, J.A.2    Benes, H.3    Cochrane, B.J.4    Zimniak, P.5
  • 35
    • 0029278802 scopus 로고
    • Glutathione S-transferases from Larval Manduca sexta Midgut: sequence of two cDNAs and enzyme induction
    • Snyder M.J., Walding J.K., and Feyereisen R. Glutathione S-transferases from Larval Manduca sexta Midgut: sequence of two cDNAs and enzyme induction. Insect Biochem. Mol. Biol. 25 (1995) 455-465
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 455-465
    • Snyder, M.J.1    Walding, J.K.2    Feyereisen, R.3
  • 36
    • 3142677326 scopus 로고    scopus 로고
    • Organisation and structural evolution of the rice glutathione S-transferase gene family
    • Soranzo N., Sari Gorla M., Mizzi L., De Toma G., and Frova C. Organisation and structural evolution of the rice glutathione S-transferase gene family. Mol. Genet. Genomics 271 (2004) 511-521
    • (2004) Mol. Genet. Genomics , vol.271 , pp. 511-521
    • Soranzo, N.1    Sari Gorla, M.2    Mizzi, L.3    De Toma, G.4    Frova, C.5
  • 38
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., and Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24 (2007) 1596-1599
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 39
    • 59649089055 scopus 로고    scopus 로고
    • Silkworm genome sequence reveals biology underlying silk production, phytophagy, and metamorphosis
    • The International Silkworm Genome Sequencing Consortium, submitted for publication
    • The International Silkworm Genome Sequencing Consortium. Silkworm genome sequence reveals biology underlying silk production, phytophagy, and metamorphosis, submitted for publication.
  • 40
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 41
    • 30344432127 scopus 로고    scopus 로고
    • Drosophila glutathione S-transferases
    • Tu C.P., and Akgul B. Drosophila glutathione S-transferases. Methods Enzymol. 401 (2005) 204-226
    • (2005) Methods Enzymol. , vol.401 , pp. 204-226
    • Tu, C.P.1    Akgul, B.2
  • 42
    • 0035397391 scopus 로고    scopus 로고
    • Glutathione S-transferases as antioxidant defence agents confer pyrethroid resistance in Nilaparvata lugens
    • Vontas J.G., Small G.J., and Hemingway J. Glutathione S-transferases as antioxidant defence agents confer pyrethroid resistance in Nilaparvata lugens. Biochem. J. 357 (2001) 65-72
    • (2001) Biochem. J. , vol.357 , pp. 65-72
    • Vontas, J.G.1    Small, G.J.2    Hemingway, J.3
  • 44
    • 0000532196 scopus 로고    scopus 로고
    • Phoxim resistance in Helicoverpa armigera (Lepidoptera: Noctuidae) in China
    • Wu K., Liang G., and Guo Y. Phoxim resistance in Helicoverpa armigera (Lepidoptera: Noctuidae) in China. J. Econ. Entomol. 90 (1997) 868-872
    • (1997) J. Econ. Entomol. , vol.90 , pp. 868-872
    • Wu, K.1    Liang, G.2    Guo, Y.3
  • 46
    • 33751031609 scopus 로고    scopus 로고
    • Identification of a Sigma-class glutathione S-transferase from the silkworm, Bombyx mori
    • Yamamoto K., Zhang P.B., Banno Y., and Fujii H. Identification of a Sigma-class glutathione S-transferase from the silkworm, Bombyx mori. J. Appl. Entomol. 130 (2006) 515-522
    • (2006) J. Appl. Entomol. , vol.130 , pp. 515-522
    • Yamamoto, K.1    Zhang, P.B.2    Banno, Y.3    Fujii, H.4
  • 47
    • 0000120689 scopus 로고
    • Detection and biochemical characterization of insecticide resistance in fall armyworm (Lepidoprera: Noctuidae)
    • Yu S.J. Detection and biochemical characterization of insecticide resistance in fall armyworm (Lepidoprera: Noctuidae). J. Econ. Entomol. 85 (1992) 675-682
    • (1992) J. Econ. Entomol. , vol.85 , pp. 675-682
    • Yu, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.