INSILICO CHARACTERIZATION OF GLUTATHIONE S-TRANSFERASES AND THEIR INTERACTION STUDY IN MULBERRY SILKWORM, BOMBYX MORI.
- Bioinformatics Center, Central Sericultural Research and Training Institute, Srirampura, Mysuru -570008, Karnataka.
14 Downloads
114 Views
Abstract
The Glutathione S-transferases are cytosolic enzymes that are found in both prokaryotes and eukaryotes. The GST multigene family are phase II detoxification enzymes that mainly helps to detoxify the large range of xenobiotic compounds in many organisms. These enzymes play a major role in detoxification pathway along with their related genes. We characterized the each GSTs class of silkworm such as Delta, Epsilon, Omega, Theta, Zeta and the phylogentic tree of GSTs were consructed. Further, we identified the conserved domains of GSTs such as thioredoxin_like and GST_C_family superfamily. Also, the G-site, H-site and dimer inferace of GSTs were identified. Around 10 conserved motifs were found by analyzing all GSTs of the silkworm. The silkworm genome sequences were mapped into the kegg pathway database and found the silkworm genes that are found in the xenobiotics metabolism pathway. Additionally, 128 protein-protein interactions of silkworm were found from the GSTs and their related genes of metabolic pathways. Further, functional enrichment analysis was shown. This study paves ways to understand the phase II detoxification enzymes, glutathione S-transferases and xenobiotics detoxification metabolic pathway of the mulberry silkworm.
Keywords
Article Analytics
References
- Aceto A., Dragani B., Melino S., Allocati N., Masulli M., Di?Ilio C., Petruzzelli R. Identification of an N-capping box that affects the α6-helix propensity in glutathione S-transferase superfamily proteins: a role for an invariant aspartic residue.?Biochem. J.?1997;322:229?234.
- Aurora R., Rose G.?D. Helix capping.Protein Science.1998;7:21?38.
- Bailey TL, Boden M, Buske FA, et al (2009) MEME Suite: Tools for motif discovery and searching. Nucleic Acids Res. 37.
- Chelvanayagam, G., Parker, M.W., Board, P.G., 2001. Fly fishing for GSTs: a unifiednomenclature for mammalian and insect glutathione transferases. Chem. Biol. 133, 256?260.
- Chiang, F.M., Sun, C.N., 1993. Glutathione transferase isozymes of diamondback moth larvae and their role in the degradation of some organophosphorus Pestic. Biochem. Physiol. 45, 7?14.
- Clark, A.G., Shamaan, N.A., 1984. Evidence that DDT-dehydrochlorinase from the house fly is a glutathione S-transferase. Pestic. Biochem. Physiol. 22, 249?261.
- Cocco R., Stenberg G., Dragani B., Rossi?Principe D., Paludi D., Mannervik B., Aceto A. The folding and stability of human alpha class glutathione transferase A1-1 depend on distinct roles of a conserved N-capping box and hydrophobic staple motif.?J. Biol. Chem.?2001;276:32177?32183.
- Ding, Y., Ortelli, F., Rossiter, L.C., Hemingway, J., Ranson, H., 2003. The Anophelesgambiae glutathione transferase supergene family: annotation, phylogeny andexpression profiles. BMC Genomics 4, 35.
- Dragani B., Stenberg G., Melino S., Petruzzelli R., Mannervik B., Aceto A. The conserved N-capping box in the hydrophobic core of glutathione S-transferase P1-1 is essential for refolding. Identification of a buried and conserved hydrogen bond important for protein stability.?J. Biol. Chem.?1997;272:25518?25523.
- Eddy SR (1998) Profile hidden Markov models. Bioinformatics 14:755?63.
- Harper E.?T., Rose G.?D. Helix stop signals in proteins and peptides: the capping box.?Biochemistry.1993;32:7605?7609.
- Hayes, J.D., Flanagan, J.U., Jowsey, I.R., 2005. Glutathione transferases. Annu. Rev. Toxicol. 45, 51?88.
- Huang, H.S., Hu, N.T., Yao, Y.E., Wu, C.Y., Chiang, S.W., Sun, C.N., 1998. Molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the diamondback moth, Plutella xylostella. Insect Mol. Biol. 28, 651?658.
- Jakobsson, P.J., Morgenstern, R., Mancini, J., Ford-Hutchinson, A., Persson, B., 1999.Common structural features of MAPEG-a widespread superfamily of membraneassociated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Sci. 8, 689?692.
- Kanehisa M, Goto S, Kawashima S, Okuno Y, Hattori M (2004) The KEGG resource for deciphering the genome. Nucleic Acids Res 32(suppl 1):D277?D280.
- Ku, C.C., Chiang, F.M., Hsin, C.Y., Yao, Y.E., Sun, C.N., 1994. Glutathione transferase isozymes involved in insecticide resistance of diamondback moth larvae. Pestic. Physiol. 50, 191?197.
- Lander, J.E., Parsons, J.F., Rife, C.L., Gilliland, G.L., Armstrong, R.N., 2004. Parallelevolutionary pathways for glutathione transferases: structure and mechanismof the mitochondrial class Kappa enzyme rGSTK1-1. Biochemistry 43, 352?361.
- Morel, F., Rauch, C., Petit, E., Piton, A., Theret, N., Coles, B., Guillouzo, A., 2004. Geneand protein characterization of the human glutathione S-transferase kappa andevidence for a peroxisomal localization. J. Biol. Chem. 279, 16246?16253.
- Motoyama, N., Dauterman, W.C., 1980. Glutathione S-transferases: their role in themetabolism of organophosphorus insecticides. Rev. Biochem. Toxicol. 2, 49?69.
- Ranson, H., Claudianos, C., Ortelli, F., Abgrall, C., Hemingway, J., Sharakhova, M.V.,Unger, M.F., Collins, F.H., Feyereisen, R., 2002. Evolution of supergene familiesassociated with insecticide resistance. Science 298, 179?181.
- Ranson, H., Rossiter, L., Ortelli, F., Jensen, B., Wang, X., Roth, C.W., Collins, F.H.,Hemingway, J., 2001. Identification of a novel class of insect glutathioneS-transferases involved in DDT resistance in the malaria vector, Anopheles gambiae. Biochem. J. 359, 295?304.
- Shannon P, et al.?Cytoscape: A Software Environment for Integrated Models of Biomolecular Interaction Networks Genome Res. 2003;13:2498.
- Sheehan, D., Meade, G., Foley, V.M., Dowd, C.A., 2001. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360, 1?16.
- Sievers F, Wilm A, Dineen D, et al (2011) Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 7:539 . doi: 10.1038/msb.2011.75.
- Singh, S.P., Coronella, J.A., Benes, H., Cochrane, B.J., Zimniak, P., 2001. Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1(GST-2) in conjugation of lipid peroxidation end products. Eur. J. Biochem. 268, 2912?2923.
- Stenberg G., Dragani B., Cocco R., Mannervik B., Aceto A. A conserved ?hydrophobic staple motif? plays a crucial role in the refolding of human glutathione transferase P1-1.?J. Biol. Chem.?2000;275:10421?10428.
- Sumathy R., Rao A.S., Chandrakanth N. et al. (2014)?In silicoidentification of protein-protein interactions in Silkworm,?Bombyx mori.?Bioinformation,?10, 56?62.
- Tamura K, Stecher G, Peterson D, et al (2013) MEGA6: Molecular Evolutionary Genetics Analysis version 6.0. Mol Biol Evol 30:2725?9 . doi: 10.1093/molbev/mst197.
- Vontas, J.G., Small, G.J., Hemingway, J., 2001. Glutathione S-transferases as antioxidant defence agents confer pyrethroid resistance in Nilaparvata lugens. Bio-chem. J. 357, 65?72.
- Wu, K., Liang, G., Guo, Y., 1997. Phoxim resistance in Helicoverpa armigera (Lepidoptera: Noctuidae) in China. J. Econ. Entomol. 90, 868?872.
- Yu, S.J., 1992. Detection and biochemical characterization of insecticide resistance in fall armyworm (Lepidoprera: Noctuidae). J. Econ. Entomol. 85, 675?682.
- Yu, Q., Lu, C., Li, B., Fang, S., Zuo, W., Dai, F., Zhang, Z., Xiang, Z., 2008. Identification, genomic organization and expression pattern of glutathione S-transferase in the silkworm, Bombyx mori. Insect Biochem Mol Biol. 38, 1158-64.
How to Cite This Article
Sumathy R, Sivaprasad V and Manthira Moorthy S. (2018); INSILICO CHARACTERIZATION OF GLUTATHIONE S-TRANSFERASES AND THEIR INTERACTION STUDY IN MULBERRY SILKWORM, BOMBYX MORI., Int. J. of Adv. Res., 6 (02), 1204-1212, ISSN 2320-5407. DOI: https://doi.org/10.21474/IJAR01/6545
Corresponding Author
This work is licensed under a Creative Commons Attribution 4.0 International License.





