This recombinant Vaccinia virus mRNA-capping enzyme catalytic subunit (VACWR106) 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.
The protein OPG113 (mRNA-capping enzyme catalytic subunit) is involved in mRNA capping, which is essential for the stability and efficient translation of mRNA. This mRNA capping enzyme catalytic subunit catalyzes the addition of a guanosine cap to the 5' end of the mRNA molecule [1]. It is recruited to the transcription complex through interactions with the phosphorylated carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II [3][4]. Additionally, the mRNA capping enzyme catalytic subunit interacts with other components of the mRNA capping pathway and the RNA polymerase II transcription complex [5].
The mRNA capping enzyme catalytic subunit plays a critical role in the formation of the 5' cap structure of eukaryotic mRNA, which is essential for mRNA stability and efficient translation [6]. Furthermore, the enzyme is involved in the process of cap snatching, where the cap structure is acquired from nascent host mRNAs, a process crucial for the initiation of transcription [7]. The mRNA capping enzyme catalytic subunit is also implicated in the targeting of the mRNA capping apparatus to the transcription elongation complex, highlighting its significance in regulating gene expression [8].
References:
[1] P. Cong and S. Shuman, Mutational analysis of mrna capping enzyme identifies amino acids involved in gtp binding, enzyme-guanylate formation, and gmp transfer to rna, Molecular and Cellular Biology, vol. 15, no. 11, p. 6222-6231, 1995. https://doi.org/10.1128/mcb.15.11.6222
[3] E. Cho, T. Takagi, C. Moore, & S. Buratowski, Mrna capping enzyme is recruited to the transcription complex by phosphorylation of the rna polymerase ii carboxy-terminal domain, Genes & Development, vol. 11, no. 24, p. 3319-3326, 1997. https://doi.org/10.1101/gad.11.24.3319
[4] N. Saha, B. Schwer, & S. Shuman, Characterization of human, schizosaccharomyces pombe, and candida albicans mrna cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes, Journal of Biological Chemistry, vol. 274, no. 23, p. 16553-16562, 1999. https://doi.org/10.1074/jbc.274.23.16553
[5] S. Wang and S. Shuman, Structure-function analysis of the mrna cap methyltransferase of saccharomyces cerevisiae, Journal of Biological Chemistry, vol. 272, no. 23, p. 14683-14689, 1997. https://doi.org/10.1074/jbc.272.23.14683
[6] C. Fàbrega, S. Hausmann, V. Shen, S. Shuman, & C. Lima, Structure and mechanism of mrna cap (guanine-n7) methyltransferase, Molecular Cell, vol. 13, no. 1, p. 77-89, 2004. https://doi.org/10.1016/s1097-2765(03)00522-7
[7] P. Palanivelu, An insight into the active sites of the catalytic basic protein subunit pb1 of the rna polymerase of human influenza viruses, World Journal of Advanced Research and Reviews, vol. 17, no. 1, p. 625-656, 2023. https://doi.org/10.30574/wjarr.2023.17.1.0109
[8] S. Hausmann, C. Vivarès, & S. Shuman, Characterization of the mrna capping apparatus of the microsporidian parasite encephalitozoon cuniculi, Journal of Biological Chemistry, vol. 277, no. 1, p. 96-103, 2002. https://doi.org/10.1074/jbc.m109649200
