In silico characterization of SAMdC from Pokkali rice and its overexpression in transgenic tobacco

, , ,

Research Articles | Published:

Print ISSN : 0970-4078.
Online ISSN : 2229-4473.
Pub Email:
Doi: 10.1007/s42535-019-00019-2
First Page: 158
Last Page: 166
Views: 688

Keywords: S-adenosylmethionine decarboxylase, Docking analysis, Pokkali rice, Polyamines, NaCl stress, Overexpression, Transgenic tobacco


Polyamines help to mitigate salt stress in plants. SAMdC or S-adenosyl methionine decarboxylase is a crucial enzyme in the polyamine biosynthetic pathway. Overexpressing the samdc gene of Pokkali (a salt-tolerant Indica rice landrace) in the model plant tobacco through Agrobacterium-mediated transformation resulted in tobacco plants capable of withstanding high salinity (200 mM) stress. The transgenic tobacco plants maintained a steady level of the higher polyamines and resisted ionic imbalance under salt stress. Since appropriate binding of the substrate with the enzyme is essential for an enzymatic reaction, we performed molecular docking experiment of SAMdC enzyme of Pokkali rice and tobacco to get an idea about its commonality in the two plants in the backdrop of Japonica rice and Arabidopsis. In silico characterization of SAMdC revealed that the enzyme used the same substrate in Pokkali rice and tobacco, from where the gene is introgressed and where it is overexpressed.

S-adenosylmethionine decarboxylase, Docking analysis, Pokkali rice, Polyamines, NaCl stress, Overexpression, Transgenic tobacco

*Pdf Download

(*Only SPR Members can download pdf file; #Open Access;)



  1. Arnon DI (1949) Copper enzymes in isolated chloroplasts: polyphenol oxidase in Beta vulgaris. Plant Physiol. 24:1–15

  2. Basu R, Mitra N, Ghosh B (1988) Salinity results in polyamine accumulation in early rice (Oryza sativa) seedlings. Aust. J. Plant Physiol. 15:777–786

  3. de Agazio M, Grego S, Ciofi-Luzzatto A, Rea E, Zaccaria ML, Federico R (1995) Inhibition of maize primary root elongation by spermidine: effect on cell shape and mitotic index. J. Plant Growth Regul. 14:85–89

  4. Gangopadhyay G, Das S, Mitra SK, Poddar R, Modak BK, Mukherjee KK (2002) Enhanced rate of multiplication and rooting through the use of coir in aseptic liquid culture media. Plant Cell Tissue Organ Cult. 68:301–310

  5. Laha S, Sen S, Ghosh B, Sengupta DN (2014) Characterization of plant S-Adenosyl-L-Methionine Decarboxylase and Spermidine Synthase in polyamine deficient mutant strain of E. coli. Int. Res. J. Biological Sci. 3:60–68

  6. Liu JH, Wang W, Wu H, Gong X, Moriguchi T (2015) Polyamines function in stress tolerance: from synthesis to regulation. Front. Plant Sci. 6:827.

  7. Liu Z, Liu P, Qi D, Peng X, Liu G (2017) Enhancement of cold and salt tolerance of Arabidopsis by transgenic expression of the S-adenosylmethionine decarboxylase gene from Leymus chinensis. J. Plant Physiol. 211:90–99

  8. Luo J, Liu M, Zhang C, Zhang P, Chen J, Guo Z, Lu S (2017) Transgenic Centipede grass (Eremochloa ophiuroides [Munro] Hack.) overexpressing S-Adenosylmethionine Decarboxylase (SAMDC) gene for improved cold tolerance through involvement of H2O2 and NO signalling. Front Plant Sci 8:1655

  9. Manni A, Fischer S, Franks M, Washington S, De Arment R, Griffith J, Demers L, Verderame M, Leiby B, Mauger D (2001) S-adenosylmethionine decarboxylase overexpression reduces invasiveness and tumorigenicity in nude mice of MCF-7 breast cancer cells. Int. J. Oncol. 2:317–323

  10. Marco F, Busó E, Carrasco P (2014) Overexpression of SAMDC1 gene in Arabidopsis thaliana increases expression of defence-related genes as well as resistance to Pseudomonas syringae and Hyaloperonospora arabidopsidis. Front. Plant Sci. 5:115.

  11. Minocha R, Majumdar R, Minocha SC (2014) Polyamines and abiotic stress in plants: a complex relationship. Front. Plant Sci. 5:175–180

  12. Murashige T, Skoog F (1962) A revised medium for rapid growth and bio assays with tobacco tissue cultures. Physiol. Plant. 15:473–497

  13. Persson K, Slund LA, Grahn B, Hanke J, Heby O (1998) Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase: characterization of the gene and the encoded enzyme. Biochem. J. 333:527–537

  14. Sambrook J, Russel DW (2001) Molecular Cloning: A Laboratory Manual Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY, USA

  15. Slocum RD (1991) Polyamine biosynthesis in plants. In: Slocum RD, Flores HE (eds) Biochemistry and Physiology of Polyamines in Plants. CRC Press, Boca Raton, FL, pp 23–40

  16. Xie JH, Zapata-Arias FJ, Shen M, Afza R (2000) Salinity tolerant performance and genetic diversity of four rice varieties. Euphytica 116:105–110

  17. Yang J, Roy A, Zhang Y (2013a) Protein-ligand binding site recognition using complementary binding-specific substructure comparison and sequence profile alignment. Bioinformatics 29:2588–2595

  18. Yang J, Roy A, Zhang Y (2013b) BioLiP: a semi-manually curated database for biologically relevant ligand-protein interactions. Nucleic Acids Res 41(database issue):D1096–D1103

  19. Yesmin N, Elias SM, Rahman MS, Haque T, Mahbub Hasan AKM, Seraj ZI (2014) Unique genotypic differences discovered among indigenous Bangladeshi rice landraces. Int J Genom. (Article ID 210328)

  20. Zhang Y (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics.



Author Information

Laha Saswati
Department of Botany, Bethune College, Kolkata, India

Kumar Diptasree
Division of Plant Biology, Bose Institute (Main Campus), Kolkata, India

Sengupta Dibyendu N.
Division of Plant Biology, Bose Institute (Main Campus), Kolkata, India

Gangopadhyay Gaurab
Division of Plant Biology, Bose Institute (Main Campus), Kolkata, India