Expression, detection of candidate function and homology modeling for Vicia villosa ornithine δ-aminotransferase
dc.Affiliation | October University for modern sciences and Arts (MSA) | |
dc.contributor.author | M.K. Nada, Ahmed | |
dc.contributor.author | M. Abd-Elhalim, Haytham | |
dc.contributor.author | M. El-Domyati, Fotouh | |
dc.contributor.author | M. I. Abou-Ali, Rania | |
dc.contributor.author | Bahieldin, Ahmed | |
dc.date.accessioned | 2020-02-02T10:40:56Z | |
dc.date.available | 2020-02-02T10:40:56Z | |
dc.date.issued | 2010 | |
dc.description | MSA Google Scholar | en_US |
dc.description.abstract | The accumulation of compatible solutes during stress in plant cell is well documented. Proline is one of these solutes that accumulates in the cytosol in response to drought or salinity stress in plants. Proline has several functions during stress just like osmotic adjustment, osmoprotection, free radical scavenger and antioxidant. Ornithine δ-aminotransferase (δ-OAT) is an important enzyme in proline biosynthetic pathway. It catalyzes the transamination of ornithine to pyrroline5-carboxylate, which can be reduced into proline. Expression of ornithine δ-aminotransferase gene isolated from Vicia villosa (VvOAT) showed protein with a molecular mass of 63 KDa, which is compatible with the predicted mass and after VvOAT gene delivery into E. coli host HB101, VvOAT gene enhanced its salt tolerance. Homology modeling of VvOAT was performed based on the crystal structure of the ornithine δ-aminotransferase from humans (PDB code 2OATA). With this model, a flexible docking study with the substrate and inhibitors was performed. The results indicated that PHE170 and ASN171 in VvOAT are the important determinant residues in binding as they have strong hydrogen bonding contacts with the substrate and inhibitors. All the obtained results indicated the efficiency of utilizing this gene in conferring salt tolerance | en_US |
dc.identifier.citation | 1. Burg MB, Kwon ED, Kultz D. Osmotic regulation of gene expression. VASEB j 1996; 10:1598-606. 2. Chen THH, Murata N. Enhancement of tolerance of abiotic stress by metabolic engineering of betaines and other compatible solutes. Curr Opin Plant Biol 2002; 5:2. 3. Yancey PH, Clark ME, Hand SC, Bowlus RD, Somero GN. Living with water stress: Evolution of osmolyte systems. Science 1982; 217:1214-22. 4. Serraj R, Sinclair TR. Osmolyte accumulation: Can it really help increase in crop yield under drought conditions? Plant Cell Environ 2002; 25:333-41. 5. Hasegawa PM, Bressan R, Zhu JK, Bohnert HJ. Plant cellular and molecular responses to high salinity. Annu Rev Plant Physiol Plant Mol Biol 2000; 51:463-99. 6. Shen B, Jensen RG, Bohnert HJ. Mannitol protects against oxidation by hyderoxyl radicals. Plant Physiol 1997; 115:527-32. 7. Hong Z, Lakkineni K, Zhang Z, Verma DPS. Removal of feedback inhibition of delta.1-pyrroline-5-carboxylate synthetase results in increased proline accumulation and protection of plants from osmotic stress. Plant Physiol 2000; 122:1129-36. 8. Akashi K, Miyake C, Yokota A. Citrulline, a novel compatible solute in drought-tolerant wild watermelon leaves, is an efficient hydroxyl radical scavenger. FEBS Leil 2001; 508:438-42. 9. Rains DW. Plant tissue and protoplast culture: application to stress physiology and biochemistry. In: Jones HG, Flowers TJ, Jones MB (Eds), Plants under Stresses: Biochemistry, Physiology and Ecology and their Application to Plant Improvement. Cambridge University Press, Cambridge 1989; 181-96. 10. Ashraf M. Breeding for salinity tolerance in plants. Crit Rev Plant Sci 1994; 13:17-42. 11. Ali G, Srivastava PS, Iqbal M. Proline accumulation, protein pattern and photosynthesis in regenerants grown under NaCl stress. Biol Plant 1999; 42:89-95. 12. Rhodes D, Verslues PE, Sharp RE. Role of amino acids in abiotic stress resistance. In: Singh BK (Ed), Plant Amino Acids: Biochemistry and Biotechnology. Marcel Dekker NY 1999; 319-56. 13. Ozturk L, Demir Y. In-vivo and in-vitro protective role of proline. Plant Growth Regul 2002; 38:259-64. 14. Hsu SY, Hsu YT, Kao CH. The effect of polyethylene glycol on proline accumulation in rice leaves. Biol Plant 2003; 46:73-8. 15. Kishor PBK, Hong Z, Miao GH, Hu CAA, Verma DPS. Overexpression of [delta]-pyrroline-5-carboxylate synthetase increases proline production and confers osmotolerance in transgenic plants. Plant Physiol 1995; 108:1387-94. 16. Srinivas V, Balasubramanian D. Proline is a proteincompatible hydrotrope. Langmuir 1995; 11:2830-3. 17. Hare PD, Cress WA. Metabolic implications of stressinduced proline accumulation in plants. Plant Growth Regul 1997; 21:79-102. 18. Hare PD, Cress WA, Staden JV. Dissecting the roles of osmolyte accumulation during stress. Plant Cell Environ 1998; 21:535-53. 19. Satoh R, Nakashima K, Seki M, Shinozaki K, Yamaguchi-Shinozaki K. ACTCAT, a novel cis-acting element for proline- and hypoosmolarity-responsive expression of the ProDH gene encoding proline dehydrogenase in Arabidopsis. Plant Physiol 2002; 130:709-19. 20. Oono Y, Seki M, Nanjo T, Narusaka M, Fujita M, Satoh R, et al. Monitoring expression profiles of Arabidopsis gene expression during rehydration process after dehydration using ca 7,000 full-length cDNA microarray. Plant J 2003; 34:868-87. 21. Ben Ahmed C, Ben Rouina B, Sensoy S, Boukhriss M, Ben Abdullah F. Exogenous proline effects on photosynthetic performance and antioxidant defense system of young olive tree. J Agric Food Chem 2010; 14:58:4216-22. 22. Roosens NH, Al Bitar F, Loenders K, Angenon G, Jacobs M. Overexpression of ornithine-δ-aminotransferase increases proline biosynthesis and confers osmotolerance in transgenic plants. Mol Breed 2002; 9:73-80. 23. Sekhar PN, Amrutha RN, Sangam S, Verma DPS, Kavi Kishor PB. Biochemical characterization, homology modeling and docking studies of ornithine δ-aminotransferase-an important enzyme in proline biosynthesis of plants. J Mol Graph Model 2007; 26:709-1924. Delauney AJ, Hu CAA, Kavi Kishor PB, Verma DPS. Cloning of ornithine δ-aminotransferase cDNA from Vigna aconitifolia by trans-complementation in Escherichia coli and regulation of proline biosynthesis. J Biol Chem 1993; 25:18673-8. 25. Hervieu F, Le Dily F, Huault C, Billard JP. Contribution of ornithine aminotransferase to proline accumulation in NaCI-treated radish cotyledons. Plant Cell Environ 1995; 18:205-10. 26. Roosens NH, Thu TT, Iskandar HM, Jacobs M. Isolation of the ornithine-δ-aminotransferase cDNA and effect of salt stress on its expression in Arabidopsis thaliana. Plant Physiol 1998; 117:263-71. 27. Abdelhalim HM, Nada AMK, El-Domyati FM, AbouAli RMI, Diab AA, Bahieldin A. Cloning, sequence analysis and in silico mapping of an ABA-inducible gene coding for ornithine δ-aminotransferase from Vicia villosa. Egyptian J of Genetics and Cytology 2010; 39:143-56. 28. Unger TF. Show me the money: prokaryotic expression vectors and purification systems. The Scientist 1997; 11:20-3. 29. Novagen. Protein Expression: Prokaryotic Expression: pETBlue and pET System Overview. Novagen 2002; 84-91.30. Gafan C, Wilson J, Berger LC, Berger BJ. Characterization of the ornithine aminotransferase from Plasmodium falciparum. Mol Biochem Parasitol 2001; 118:1-10. 31. Stránská J, Snegaroff J, Chamrád I, Lenobel R, Šebela M. Cloning, expression and purification of plant ornithine delta aminotransferase. Comparative Biochemistry and Physiology 2009; 153:159-64. 32. Edris S, Bahieldin A, Domyati FM, Youins RAA, Hassanein H. Characterization of glycerol-3-phosphate dehydrogenase (GPD1) gene from Egyptian yeast with fluorescence differential display. Egyptian J of Genetics and Cytology 2009; 38:29-42. 33. Storici P, Capitani G, Muller R, Schirmer T, Jansonius JN. Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine. J Mol Biol 1999; 285:297-309. 34. Marti-Renom MA, Stuart AC, Fiser A, Sanchez R, Melo F, Sali A. Comparative protein structure modeling of genes and genomes. Annu Rev Biophys Biomol Struct 2000; 29:291-325.35. Eswar N, John B, Mirkovic N, Fiser A, Ilyin VA, Pieper U, et al. Tools for comparative protein structure modeling and analysis. Nucleic Acids Res 2003; 31:3375-80. 36. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol 1990; 215:403-10. 37. Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997; 50:3389-402. 38. Mizuguchi K, Deane CM, Blundell TL, Johnson MS, Overington JP. JOY: protein sequence-structure representation and analysis. Bioinformatics 1998; 14:617-23. 39. Sheik SS, Sundararajan P, Hussain ASZ, Sekar K. Ramachandran plot on the web. Bioinformatics 2002; 18:1548-9. | en_US |
dc.identifier.issn | 1938-1999 (Print) | |
dc.identifier.issn | 1938-2006 (Online) | |
dc.identifier.uri | https://cutt.ly/rtyvNCL | |
dc.language.iso | en | en_US |
dc.publisher | Taylor & Francis | en_US |
dc.relation.ispartofseries | GM crops;1:4, 250-256 | |
dc.subject | proline | en_US |
dc.subject | δ-aminotransferase | en_US |
dc.subject | SDS-PAGE | en_US |
dc.subject | bacterial transformation | en_US |
dc.subject | homology modeling | en_US |
dc.subject | salt tolerance | en_US |
dc.title | Expression, detection of candidate function and homology modeling for Vicia villosa ornithine δ-aminotransferase | en_US |
dc.type | Article | en_US |
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