SPOUT domain-containing methyltransferase 1 (SPOUT1)

SPOUT domain-containing methyltransferase 1 (SPOUT1), also known as CENP-32 or C9orf114, is a SAM-dependent RNA methyltransferase belonging to the SPOUT superfamily, characterized by a deeply knotted trefoil fold and a specific OB-fold insertion involved in nucleic acid recognition[1][2]. It acts primarily to catalyze N3 methylation of uridine residues in 28S rRNA, using S-adenosyl-L-methionine (SAM) as the methyl group donor[1]. SPOUT1 is crucial for the assembly of the mitotic spindle and proper chromosome segregation, mediated by its methyltransferase activity and its role in tethering centrosomes to spindle poles in dividing cells[1]. Bi-allelic variants of SPOUT1 are associated with neurodevelopmental disorders and defects in mitosis in model organisms, indicating its importance for cell division and neural development[1]. No currently approved drugs directly target this enzyme, and there are no well-established clinical biomarkers. As a member of the SPOUT methyltransferase family, it is structurally and functionally distinct from other methyltransferases, with the SPOUT domain contributing to both catalysis and nucleic acid substrate recognition[1][2].

Other names

28S rRNA (uridine-N(3))-methyltransferaseC9orf114CENP-32HSPC109Centromere protein 32Kinetochore-associated proteinMethyltransferase C9orf114Ribosomal RNA methyltransferase SPOUT1putative methyltransferase C9orf114NEDGSB

S-adenosyl-L-methionine (SAM)-dependent methyl group transfer to rRNA (N3 methylation of uridine in 28S rRNA)