{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fujita S"],"funding":["Institute for Fermentation Osaka","Ehime University","Japan Society for the Promotion of Science"],"pagination":["107505"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11298593"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["300(8)"],"pubmed_abstract":["Archaeosine (G<sup>+</sup>) is an archaea-specific tRNA modification synthesized via multiple steps. In the first step, archaeosine tRNA guanine transglucosylase (ArcTGT) exchanges the G15 base in tRNA with 7-cyano-7-deazaguanine (preQ<sub>0</sub>). In Euryarchaea, preQ<sub>0</sub>15 in tRNA is further modified by archaeosine synthase (ArcS). Thermococcus kodakarensis ArcS catalyzes a lysine-transfer reaction to produce preQ<sub>0</sub>-lysine (preQ<sub>0</sub>-Lys) as an intermediate. The resulting preQ<sub>0</sub>-Lys15 in tRNA is converted to G<sup>+</sup>15 by a radical S-adenosyl-L-methionine enzyme for archaeosine formation (RaSEA), which forms a complex with ArcS. Here, we focus on the substrate tRNA recognition mechanism of ArcS. Kinetic parameters of ArcS for lysine and tRNA-preQ<"],"journal":["The Journal of biological chemistry"],"pubmed_title":["ArcS from Thermococcus kodakarensis transfers L-lysine to preQ<sub>0</sub> nucleoside derivatives as minimum substrate RNAs."],"pmcid":["PMC11298593"],"funding_grant_id":["JP24K09381","JP20H03211","G-2022-2-052"],"pubmed_authors":["Fujita S","Yamagami R","Yokogawa T","Hirata A","Oka N","Hori H","Kawamura T","Sugio Y"],"additional_accession":[]},"is_claimable":false,"name":"ArcS from Thermococcus kodakarensis transfers L-lysine to preQ<sub>0</sub> nucleoside derivatives as minimum substrate RNAs.","description":"Archaeosine (G<sup>+</sup>) is an archaea-specific tRNA modification synthesized via multiple steps. In the first step, archaeosine tRNA guanine transglucosylase (ArcTGT) exchanges the G15 base in tRNA with 7-cyano-7-deazaguanine (preQ<sub>0</sub>). In Euryarchaea, preQ<sub>0</sub>15 in tRNA is further modified by archaeosine synthase (ArcS). Thermococcus kodakarensis ArcS catalyzes a lysine-transfer reaction to produce preQ<sub>0</sub>-lysine (preQ<sub>0</sub>-Lys) as an intermediate. The resulting preQ<sub>0</sub>-Lys15 in tRNA is converted to G<sup>+</sup>15 by a radical S-adenosyl-L-methionine enzyme for archaeosine formation (RaSEA), which forms a complex with ArcS. Here, we focus on the substrate tRNA recognition mechanism of ArcS. Kinetic parameters of ArcS for lysine and tRNA-preQ<","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2025-04-26T05:37:47.724Z","creation":"2025-04-06T11:32:39.548Z"},"accession":"S-EPMC11298593","cross_references":{"pubmed":["38944122"],"doi":["10.1016/j.jbc.2024.107505"]}}