This FMT protein is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
FMT is an essential enzyme involved in the formylation of the initiator methionyl-tRNA (Met-tRNAi) during protein synthesis in various organisms, including eubacteria, mitochondria, and chloroplasts [1][2]. This formylation process generates formylmethionyl-tRNA (fMet-tRNAi), which is crucial for the initiation of protein synthesis [1][2]. MTF catalyzes the transfer of the formyl group from N 10 -formyltetrahydrofolate to L-methionyl-tRNA, thereby forming fMet-tRNAi [3][1][4].
The formylation of the initiator tRNA by FMT is specific to the Met-tRNAi, a key step in targeting the initiator tRNA to the translation start machinery in prokaryotes [5]. This formylation reaction is significant for preventing the incorporation of methionine esterified to tRNA into elongating peptide chains [6]. Additionally, the interaction between the formylated initiator tRNA (fMet-tRNAi) and initiation factors like IF2 is crucial for initiating translation [7].
Studies have shown that disruption or mutations in the gene encoding FMT severely impair growth in organisms like Escherichia coli, highlighting the essential role of FMT in protein synthesis [8]. Furthermore, the formylation of the initiator tRNA by FMT is not essential in all eubacteria, indicating variability in the requirement for formylation among different organisms [9].
References:
[1] C. Köhrer and U. RajBhandary, Expression of escherichia coli methionyl-trna formyltransferase in saccharomyces cerevisiae leads to formylation of the cytoplasmic initiator trna and possibly to initiation of protein synthesis with formylmethionine, Molecular and Cellular Biology, vol. 22, no. 15, p. 5434-5442, 2002. https://doi.org/10.1128/mcb.22.15.5434-5442.2002
[2] V. Ramesh, S. Gite, Y. Li, & U. RajBhandary, Suppressor mutations in
escherichia coli methionyl-trna formyltransferase: role of a 16-amino acid insertion module in initiator trna recognition, Proceedings of the National Academy of Sciences, vol. 94, no. 25, p. 13524-13529, 1997. https://doi.org/10.1073/pnas.94.25.13524
[3] S. Gite and U. RajBhandary, Functional interaction of an arginine conserved in the sixteen amino acid insertion module of escherichia coli methionyl-trna formyltransferase with determinants for formylation in the initiator trna, Biochemistry, vol. 37, no. 45, p. 15925-15932, 1998. https://doi.org/10.1021/bi981873x
[4] Y. Li, W. Holmes, D. Appling, & U. RajBhandary, Initiation of protein synthesis in saccharomyces cerevisiae mitochondria without formylation of the initiator trna, Journal of Bacteriology, vol. 182, no. 10, p. 2886-2892, 2000. https://doi.org/10.1128/jb.182.10.2886-2892.2000
[5] E. Schmitt, S. Blanquet, & Y. Mechulam, Structure of crystalline escherichia coli methionyl-trna(f)met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase., The Embo Journal, vol. 15, no. 17, p. 4749-4758, 1996. https://doi.org/10.1002/j.1460-2075.1996.tb00852.x
[6] J. Guillon, Y. Mechulam, S. Blanquet, & G. Fayat, Importance of formylability and anticodon stem sequence to give a trna(met) an initiator identity in escherichia coli, Journal of Bacteriology, vol. 175, no. 14, p. 4507-4514, 1993. https://doi.org/10.1128/jb.175.14.4507-4514.1993
[7] S. Thanedar, N. Kumar, & U. Varshney, The fate of the initiator trnas is sensitive to the critical balance between interacting proteins, Journal of Biological Chemistry, vol. 275, no. 27, p. 20361-20367, 2000. https://doi.org/10.1074/jbc.m001238200
[8] J. Guillon, Y. Mechulam, J. Schmitter, S. Blanquet, & G. Fayat, Disruption of the gene for met-trna(fmet) formyltransferase severely impairs growth of escherichia coli, Journal of Bacteriology, vol. 174, no. 13, p. 4294-4301, 1992. https://doi.org/10.1128/jb.174.13.4294-4301.1992
[9] D. Newton, C. Creuzenet, & D. Mangroo, Formylation is not essential for initiation of protein synthesis in all eubacteria, Journal of Biological Chemistry, vol. 274, no. 32, p. 22143-22146, 1999. https://doi.org/10.1074/jbc.274.32.22143
