The Role of Phytochelatin Synthase in Phytoremediation Agent: Structural Conservation of Phytochelatin (PC) Synthase to Maintain Its Activity as Heavy Metal Detoxification in Plant
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Vidayanti, V. and Permatasari, G. W. . (2020) “The Role of Phytochelatin Synthase in Phytoremediation Agent: Structural Conservation of Phytochelatin (PC) Synthase to Maintain Its Activity as Heavy Metal Detoxification in Plant ”, Bioinformatics and Biomedical Research Journal, 3(2), pp. 9–14. Available at: http://bbrjournal.com/index.php/bbrj/article/view/98 (Accessed: 8December2021).

Abstract

Phytochelatin (PC) Enzyme has crucial role in heavy metal detoxification and homeostasis in plants. This study aimed to evaluate the genetic variation of PC synthase related to its activity based on structural comparison. We evaluated PC genes and protein sequences from 6 plants namely, Brassica sp., Amaranthus sp., Noccaea sp., Arabidopsis sp., Nicotiana sp., and Pteris sp. All sequences were aligned based on CLUSTALW matrix for DN sequences and MUSCLE algorithm for protein sequences. Data were clustered using MEGA Software for similarity clustering. Selected data were further modeled using SWISSMODEL to evaluate the 3D-structural analysis based on homology modeling. Thus, all protein models were superimposed and evaluated the structure comparison based on RMSD data. The result showed that genetic variation of PC gene is high among species. But it is clustered for the same species has similar sequence. In addition, protein sequences also showed the high diversity among species and it is still clustered based on their genus. RMSD data showed that PC synthase from 6 plant has similar structure and tend to conserved even there is genetic variation or amino acid modification. We concluded that structural of PC gene is more conserved than its sequences. It is important to keep its function among species.

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References

Liu S, Yang B, Liang Y, Xiao Y, Fang J (2020) Prospect of Phytoremediation Combined With Other Approaches For Remediation Of Heavy Metal-Polluted Soils. Environ. Sci. Pollut. Res. 27(14): 16069–16085. doi: 10.1007/s11356-020- 08282-6.

Shah V, Daverey A (2020) Phytoremediation: A Multidisciplinary Approach To Clean Up Heavy Metal Contaminated Soil. Environ. Technol. In-nov.18: 100774. doi: 10.1016/j.eti.2020.100774.

Filiz E, Saracoglu I, Ozyigit I, Yalcin B (2019) Comparative Analyses Of Phytochelatin Syn-thase (PCS) Genes In Higher Plants. Biotechnol. Biotechnol. Equip. 33(1): 178– 194. doi: 10.1080/13102818.2018.1559096.

Wang F, Wang Z, Zhu C (2012) Heteroexpres-sion Of The Wheat Phytochelatin Synthase Gene (Tapcs1) In Rice Enhances Cadmium Sensitivi-ty. Acta Biochim. Biophys. Sin. (Shanghai) 44(10): 886–893. doi: 10.1093/abbs/gms073.

Grill E, Mishra S, Srivastava S, Tripathi R (2007) Role Of Phytochelatins In Phytoremedia-tion Of Heavy Metals. Environmental Bioreme-diation Technologies, Springer Berlin Heidel-berg. pp. 101–146.

Fan W. et al. (2018) Two Mulberry Phytochela-tin Synthase Genes Confer Zinc/Cadmium Tol-erance And Accumulation In Transgenic Ara-bidopsis And Tobacco. Gene 645: 95–104. doi: 10.1016/j.gene.2017.12.042.

Li A. et al. (2009) Characterization of the Ses-bania rostrata Phytochelatin Synthase Gene: Al-ternative Splicing and Function of Four Isoforms. Int. J. Mol. Sci. 10(8): 3269– 3282. doi: 10.3390/ijms10083269.

Liu Z. et al. (2012) Heterologous Expression Of A Nelumbo Nucifera Phytochelatin Synthase Gene Enhances Cadmium Tolerance In Ara-bidopsis Thaliana. Appl. Biochem. Biotechnol. 166(3): 722–734. doi: 10.1007/s12010-011-9461-2.

Ha S. et al. (1999) Phytochelatin Synthase Genes From Arabidopsis And The Yeast Schiz-osaccharomyces pombe. Plant Cell 11, pp. 1153–1164.

Tsuji N. et al. (2005) Comparative Analysis Of The Two-Step Reaction Catalyzed By Prokary-otic And Eukaryotic Phytochelatin Synthase By An Ion-Pair Liquid Chromatography Assay. Planta 222, pp. 181–191.

Vivares D, Arnoux P, Pignol D (2005) A Papain-Like Enzyme At Work: Native And Acyl-Enzyme Intermediate Structures In Phytochela-tin Synthesis. Proc Natl Acad Sci 102, pp.18848–18853.

McGrath S, Zhao F (2003) Phytoextraction Of Metals And Metalloids From Contaminated Soils. Current Opinion in Biotechnology 14(3): 277–282. doi: 10.1016/S0958- 1669(03)00060

Memon A (2020) Heavy Metal-Induced Gene Expression In Plants. Contaminants In Agricul-ture: Sources, Impacts And Management. Springer International Publishing, pp. 143–173.

Lekeux G. et al. (2018) Di-Cysteine Motifs In The C-Terminus Of Plant HMA4 Proteins Con-fer Nanomolar Affinity For Zinc And Are Es-sential For HMA4 Function In Vivo. J. Exp. Bot. 69(22): 5547–5560. doi: 10.1093/jxb/ery311.

Wang J. et al. (2019) A Repeat Region From The Brassica juncea HMA4 Gene BJHMA4R Is Specifically Involved In Cd 2+ Binding In The Cytosol Under Low Heavy Metal Concentra-tions. BMC Plant Biol.19(1): 89. doi: 10.1186/s12870-019- 1674-5.

Li, D. et al. (2015) Genome-Wide Analysis And Heavy Metalinduced Expression Profiling Of The HMA Gene Family in Populus trichocarpa. Front. Plant Sci. 6(DEC): 1149. doi: 10.3389/fpls.2015.01149.

Memon, A, Zahirovic E. (2014) Genomics and Transcriptomics Analysis of Cu Accumulator Plant Brassica nigra L. http://www.arabidopsis.org/.

Goldman N, Thorne J, and Jones D (1998) As-sessing The Impact Of Secondary Structure And Solvent Accessibility On Protein Evolution. Ge-netics 149(1): 445–458. https://pmc/articles/PMC%201460119/?report=abstract

Thorne J, Goldman N, Jones D (1996) Combin-ing Protein Evolution And Secondary Structure. Mol. Biol. Evol. 13(5): 666–673. doi:10.1093/oxfordjournals.molbev.a02562

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