mRNA cap guanine-N7 methyltransferase, RG7MT1, mRNA (guanine-N(7)-)-methyltransferase, mRNA cap methyltransferase, hCMT1, hMet, hcm1p, RNMT, KIAA0398, MET, RG7MT1, hCMT1c, DKFZp686H1252.
RNMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-476 a.a.) and having a molecular mass of 57kDa.
RNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
mRNA cap guanine-N7 methyltransferase, RG7MT1, mRNA (guanine-N(7)-)-methyltransferase, mRNA cap methyltransferase, hCMT1, hMet, hcm1p, RNMT, KIAA0398, MET, RG7MT1, hCMT1c, DKFZp686H1252.
RNMT is a protein encoded by the RNMT gene in humans. The enzyme consists of 476 amino acids and has a molecular weight of approximately 55 kDa . The catalytic domain of RNMT lies between residues 121–476, and this domain is conserved in sequence, structure, and function across various eukaryotic species . The N-terminal domain (1–120 amino acids) is not required for catalytic activity but plays a regulatory role by facilitating the recruitment of RNMT to RNA polymerase II transcription initiation sites .
The capping process of mRNA involves three sequential enzymatic activities: triphosphatase, guanylyltransferase, and methyltransferase . RNMT catalyzes the final step of this process, where it transfers a methyl group from S-adenosyl methionine (AdoMet) to the N7 position of the guanine nucleotide, forming the mature cap structure, 7-methylguanosine (m7GpppN) . This cap structure is critical for the recognition of mRNA by the cap-binding complex and eukaryotic initiation factor 4F, which are involved in splicing, export, and translation initiation .
The 5’ cap structure of mRNA is essential for several cellular processes:
RNMT has been implicated in the proliferation of cancer cells and is considered a potential target for the development of anticancer therapeutics . Additionally, coronaviruses mimic the capping process of mRNA to evade the human immune system, making RNMT a target for the development of antiviral therapeutics . The enzyme’s role in mRNA stability and translation makes it a critical factor in cellular growth and proliferation.
Recent studies have focused on the kinetic characterization of human RNMT and the development of assays for high-throughput screening of potential inhibitors . These efforts aim to discover chemical probes and inhibitors that can be used to further investigate the roles of RNMT in cancer and viral infections .