RNA guanylyltransferase and 5'-phosphatase (RNGTT)

RNA guanylyltransferase and 5'-phosphatase (RNGTT) is a bifunctional enzyme critical in mRNA capping, catalyzing the first two steps in 7-methylguanosine cap formation on nascent pre-mRNAs. The N-terminal domain exhibits RNA 5'-triphosphatase activity, removing the γ-phosphate from the 5'-triphosphate end of emerging mRNA to yield a diphosphate, while the C-terminal domain displays mRNA guanylyltransferase activity, transferring GMP from GTP to the 5'-diphosphate mRNA, forming the cap structure. This cap promotes RNA stability, efficient splicing, export, and translation. RNGTT localizes primarily in the nucleoplasm, functions in essential cellular mRNA processing pathways, and is also involved in viral mRNA processing during infection. Mutations in RNGTT are associated with congenital dyserythropoietic anemia type IIIa, and its essential role in mRNA metabolism makes it a potential target in fields such as antiviral therapy and gene expression modulation[1][2][3][4].

Other names

mRNA-capping enzymemRNA 5'-triphosphate monophosphatasemRNA guanylyltransferaseCAP1AGTaseHCEHCE1hCAPHCAP1GTP--RNA guanylyltransferasemRNA 5'-phosphatasePolynucleotide 5'-triphosphataseTPase

Inhibition or modulation of mRNA capping