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Zain, Che Radziah Md.
- Isolation and Characterization of Encoded Formaldehyde Responsive Gene from the Plant Dieffenbachia compacta
Authors
1 Environmental Health and Industrial Safety Program, Universiti Kebangsaan Malaysia, Jalan Raja Muda Abdul Aziz, 50300, Kuala Lumpur, MY
2 School of Environment & Natural Resource Sciences, Universiti Kebangsaan Malaysia, 43600, Bangi, Selangor, MY
Source
Nature Environment and Pollution Technology, Vol 14, No 2 (2015), Pagination: 435-438Abstract
Plants have several defence mechanisms to survive in a stressful environment. Formaldehyde is one of the indoor air pollutants that can cause cancer. Ornamental plant Dieffenbachia compacta can be used as biological control for pollutants in the indoor air environment. This study was conducted to isolate the genes that response for detoxifying formaldehyde in have several defence mechanisms to survive in a stressful environment. Formaldehyde is one of the indoor air pollutants that can cause cancer. Ornamental plant Dieffenbachia compacta can be used as biological control for pollutants in the indoor air environment. This study was conducted to isolate the genes that response for detoxifying formaldehyde in Dieffenbachia compacta. Methods used to isolate the gene is by using reverse transcription PCR (RT-PCR). A total of 735 base pairs was isolated using a primer from Epipremnum aureum FALDH genes. Nucleotide sequence analysis showed that the sequence similarities of 85% and 84% to the FALDH mRNA for Epipremnum aureum and Populus trichocarpa respectively. While for amino acid 92% similarities were found against Epipremnum aureum and Populus trichocarpa. A total of 87 amino acids that were encoded from 261 base pairs using the Open Reading Frame Finder. Our finding showed that the isolated Dieffenbachia compacta gene is the gene for glutathione-dependent formaldehyde dehydrogenase (FALDH). As a conclusion, formaldehyde metabolism in plants is regulated by the enzyme glutathione-dependent formaldehyde dehydrogenase (FALDH). The activity of FALDH indicates that this enzyme might be part of the universal metabolism pathway shared by a variety of organisms.