{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Stonkus J"],"funding":["Research Council of Lithuania"],"pagination":["gkaf1379"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12709175"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["53(22)"],"pubmed_abstract":["Nucleoside 2'-O-methylation is a widespread RNA modification found across diverse RNA types in all domains of life. Although considerable progress has been made in mapping 2'-O-methylation sites and elucidating their biological roles, the enzymatic pathways responsible for the catabolism of 2'-O-methylated nucleosides remain largely unexplored. Here, we report a previously unidentified 2'-O-methylated nucleoside demethylation reaction catalyzed by a metagenome-derived bacterial dioxygenase named FJS. We further show that FJS-related enzymes, including human phytanoyl-CoA dioxygenase domain-containing protein 1 (PHYHD1), catalyze the 2-oxoglutarate-dependent demethylation of a broad range of ribose-methylated nucleosides, but do not act on modified nucleotides or 3'-terminal 2'-O-methylated"],"journal":["Nucleic acids research"],"pubmed_title":["A new role for PHYHD1 and related dioxygenases: demethylation of 2'-O-methylated nucleosides."],"pmcid":["PMC12709175"],"funding_grant_id":["S-MIP-24-50"],"pubmed_authors":["Rutkiene R","Jasiuniene M","Kaliniene L","Lazutka J","Meskys R","Aucynaite A","Vilkaitis G","Stonkus J","Balciunas D","Meskiene R"],"additional_accession":[]},"is_claimable":false,"name":"A new role for PHYHD1 and related dioxygenases: demethylation of 2'-O-methylated nucleosides.","description":"Nucleoside 2'-O-methylation is a widespread RNA modification found across diverse RNA types in all domains of life. Although considerable progress has been made in mapping 2'-O-methylation sites and elucidating their biological roles, the enzymatic pathways responsible for the catabolism of 2'-O-methylated nucleosides remain largely unexplored. Here, we report a previously unidentified 2'-O-methylated nucleoside demethylation reaction catalyzed by a metagenome-derived bacterial dioxygenase named FJS. We further show that FJS-related enzymes, including human phytanoyl-CoA dioxygenase domain-containing protein 1 (PHYHD1), catalyze the 2-oxoglutarate-dependent demethylation of a broad range of ribose-methylated nucleosides, but do not act on modified nucleotides or 3'-terminal 2'-O-methylated","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-08T03:19:57.943Z","creation":"2026-06-08T03:09:15.586Z"},"accession":"S-EPMC12709175","cross_references":{"pubmed":["41404801"],"doi":["10.1093/nar/gkaf1379"]}}