Team:BGIC-Global/Project
Why FORMALDEHUNTER?
Formaldehyde (HCHO) is a highly toxic compound due to nonspecific reactivity with proteins and nucleic acids [1]. It is liberated as a result of demethylation reactions in mammals [2] or from environmental sources [3], and it is a central intermediate upon growth of methylotrophic bacteria on one-carbon substrates like methanol or methane [4]. And it is widely used as a raw material in a variety of chemical products, such as resins, as well as a preservative for cosmetics, detergents, and human cadavers and animal organs for research [5]. Degradation of formaldehyde is necessary to prevent environmental pollution. Although a number of technologies are available to remove or degrade formaldehyde in its liquid pollution, biological methods are desirable because they are safe and relatively inexpensive. The most widespread enzymatic system for the conversion of formaldehyde is the glutathione (GSH)1-linked oxidation pathway, which has been found in bacteria [6]. And in recent years it is well-known for efforts to expand the synthetic biology toolbox have focused on characterizing a range of biosensors [7] and engineering existing regulators [8] to respond to new effectors. Therefore, with gene gfa have been found in Paracoccus denitrificans, we have a deep thought with degradation of formaldehyde. In our project, we hope topically make application of gene gfa with Nanoluc (formerly GFP) expression system to results on a safety and inexpensive biological method.
Reference:
1. Grafstrom, R. C., Fornace, A. J. Jr., Autrup, H., Lechner, J. F., and Harris, C. C. (1983) Science 220, 216–218
2. Jones, D. P., Thor, H., Andersson, B., and Orrenius, S. (1978) J. Biol. Chem. 253, 6031–6037
3. Zimmerman, P. R., Chatfield, R. B., Fishman, J., Crutzen, P., and Hanst, P. L. (1978) Geophys. Res. Lett. 5, 679–682
4. Vorholt, J. A., Chistoserdova, L., Stolyar, S. M., Thauer, R. K., and Lidstrom, M. E. (1999) J. Bacteriol. 181, 5750–5757
5. Yonemitsu H, Kikuchi Y. Biodegradation of high concentrations of formaldehyde using Escherichia coli expressing the formaldehyde dismutase gene of Methylobacterium sp. FD1.[J]. Biosci Biotechnol Biochem, 2017, 82(1):1-8.
6. Goenrich M, Bartoschek S, Hagemeier C H, et al. A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy[J]. Journal of Biological Chemistry, 2002, 277(5):3069-72.
7. Rogers, J. K., Guzman, C. D., Taylor, N. D., Raman, S., Anderson, K., and Church, G. M. (2015) Synthetic biosensors for precise gene control and real-time monitoring of metabolites. Nucleic Acids Res. 43, 7648−7660.
8. Taylor, N. D., Garruss, A. S., Moretti, R., Chan, S., Arbing, M., Cascio, D., Rogers, J. K., Isaacs, F. J., Kosuri, S., Baker, D., Fields, S., Church, G. M., and Raman, S. (2016) Engineering an allosteric transcription factor to respond to new ligands. Nat. Methods 13, 177−183.
Reference:
1. Grafstrom, R. C., Fornace, A. J. Jr., Autrup, H., Lechner, J. F., and Harris, C. C. (1983) Science 220, 216–218
2. Jones, D. P., Thor, H., Andersson, B., and Orrenius, S. (1978) J. Biol. Chem. 253, 6031–6037
3. Zimmerman, P. R., Chatfield, R. B., Fishman, J., Crutzen, P., and Hanst, P. L. (1978) Geophys. Res. Lett. 5, 679–682
4. Vorholt, J. A., Chistoserdova, L., Stolyar, S. M., Thauer, R. K., and Lidstrom, M. E. (1999) J. Bacteriol. 181, 5750–5757
5. Yonemitsu H, Kikuchi Y. Biodegradation of high concentrations of formaldehyde using Escherichia coli expressing the formaldehyde dismutase gene of Methylobacterium sp. FD1.[J]. Biosci Biotechnol Biochem, 2017, 82(1):1-8.
6. Goenrich M, Bartoschek S, Hagemeier C H, et al. A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy[J]. Journal of Biological Chemistry, 2002, 277(5):3069-72.
7. Rogers, J. K., Guzman, C. D., Taylor, N. D., Raman, S., Anderson, K., and Church, G. M. (2015) Synthetic biosensors for precise gene control and real-time monitoring of metabolites. Nucleic Acids Res. 43, 7648−7660.
8. Taylor, N. D., Garruss, A. S., Moretti, R., Chan, S., Arbing, M., Cascio, D., Rogers, J. K., Isaacs, F. J., Kosuri, S., Baker, D., Fields, S., Church, G. M., and Raman, S. (2016) Engineering an allosteric transcription factor to respond to new ligands. Nat. Methods 13, 177−183.