Polynucleotide 5'-hydroxyl-kinase NOL9 (NOL9)

Polynucleotide 5'-hydroxyl-kinase NOL9 (NOL9) is a non-ribosomal nucleolar enzyme that catalyzes the phosphorylation of the 5'-hydroxyl groups on RNA and DNA strands, a critical step in the maturation of ribosomal RNA. NOL9 preferentially associates with pre-60S ribosomal particles, and its kinase activity is necessary for efficient processing of large ribosomal subunit rRNAs, particularly facilitating conversion of precursor 32S rRNA into mature 5.8S(S) and 28S rRNAs. It forms a functional complex with LAS1L, combining endonuclease and kinase activities to mediate pre-rRNA cleavage and maturation. NOL9 is essential for ribosome biogenesis, cell proliferation, and normal development, as established by loss-of-function studies in animal models. Mutations or dysregulation of NOL9 are linked to rare genetic diseases and may play a role in cancer and ribosomopathies. No therapeutically approved drugs directly target NOL9, and inhibition would likely have broad and severe biological consequences due to its fundamental role in ribosome formation[1][2][3][5][6].

Other names

Nucleolar protein 9NET6Grc3FLJ23323polynucleotide 5'-hydroxyl-kinase NOL9polynucleotide 5'-kinase

Theoretical: Inhibition of NOL9 would interfere with the phosphorylation step in rRNA processing, resulting in defective ribosome biogenesis and altered protein synthesis[1][3][5].