{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Toubdji S"],"funding":["Deutsche Forschungsgemeinschaft (DFG)","Agence Nationale de la Recherche (ANR)","Agence Nationale de la Recherche","Deutsche Forschungsgemeinschaft","Science Ministry | Forskerakademiet (Danish Research Academy)","Animal Health and Welfare ERA-Net","Animal Health and Welfare ERA-Net (ANIHWA)","NIGMS NIH HHS","Science Ministry | Forskerakademiet"],"pagination":["e2401981121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11317573"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(32)"],"pubmed_abstract":["Dihydrouridine (D), a prevalent and evolutionarily conserved base in the transcriptome, primarily resides in tRNAs and, to a lesser extent, in mRNAs. Notably, this modification is found at position 2449 in the <i>Escherichia coli</i> 23S rRNA, strategically positioned near the ribosome's peptidyl transferase site. Despite the prior identification, in <i>E. coli</i> genome, of three dihydrouridine synthases (DUS), a set of NADPH and FMN-dependent enzymes known for introducing D in tRNAs and mRNAs, characterization of the enzyme responsible for D2449 deposition has remained elusive. This study introduces a rapid method for detecting D in rRNA, involving reverse transcriptase-blockage at the rhodamine-labeled D2449 site, followed by PCR amplification (RhoRT-PCR). Through analysis of rRNA from"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Exploring a unique class of flavoenzymes: Identification and biochemical characterization of ribosomal RNA dihydrouridine synthase."],"pmcid":["PMC11317573"],"funding_grant_id":["GM132254","439669440 - TRR-319-TP C01 and HE 3397/21-1","FNU-rammebevilling 10-084554","20-CE92-0030","R01 GM132254"],"pubmed_authors":["Baharoglu Z","Sudol C","Hardy L","Hamdane D","Goyenvalle C","Bregeon D","Toubdji S","de Crecy-Lagard V","Thullier Q","Douthwaite S","Helm M","Marchand V","Jean-Jean O","Rose S","Kilz LM","Yuan Y","Motorin Y"],"additional_accession":[]},"is_claimable":false,"name":"Exploring a unique class of flavoenzymes: Identification and biochemical characterization of ribosomal RNA dihydrouridine synthase.","description":"Dihydrouridine (D), a prevalent and evolutionarily conserved base in the transcriptome, primarily resides in tRNAs and, to a lesser extent, in mRNAs. Notably, this modification is found at position 2449 in the <i>Escherichia coli</i> 23S rRNA, strategically positioned near the ribosome's peptidyl transferase site. Despite the prior identification, in <i>E. coli</i> genome, of three dihydrouridine synthases (DUS), a set of NADPH and FMN-dependent enzymes known for introducing D in tRNAs and mRNAs, characterization of the enzyme responsible for D2449 deposition has remained elusive. This study introduces a rapid method for detecting D in rRNA, involving reverse transcriptase-blockage at the rhodamine-labeled D2449 site, followed by PCR amplification (RhoRT-PCR). Through analysis of rRNA from","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2026-05-02T14:33:14.224Z","creation":"2025-04-04T14:04:35.625Z"},"accession":"S-EPMC11317573","cross_references":{"pubmed":["39078675"],"doi":["10.1073/pnas.2401981121"]}}