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http://purl.uniprot.org/citations/18664566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18664566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18664566http://www.w3.org/2000/01/rdf-schema#comment"The wobble uridine in yeast cytosolic tRNA(Lys2)(UUU) and tRNA(Glu3)(UUC) undergoes a thio-modification at the second position (s(2) modification) and a methoxycarbonylmethyl modification at the fifth position (mcm(5) modification). We previously demonstrated that the cytosolic and mitochondrial iron-sulfur (Fe/S) cluster assembly machineries termed CIA and ISC, including a cysteine desulfurase called Nfs1, were essential for the s(2) modification. However, the cytosolic component that directly participates in this process remains unclear. We found that ubiquitin-like protein Urm1 and ubiquitin-activating enzyme-like protein Uba4, as well as Tuc1 and Tuc2, were strictly required for the s(2) modification. The carboxyl-terminal glycine residue of Urm1 was critical for the s(2) modification, indicating direct involvement of the unique ubiquitin-related system in this process. We also demonstrated that the s(2) and mcm(5) modifications in cytosolic tRNAs influence each other's efficiency. Taken together, our data indicate that the s(2) modification of cytosolic tRNAs is a more complex process that requires additional unidentified components."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m804043200"xsd:string
http://purl.uniprot.org/citations/18664566http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m804043200"xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/author"Hayashi H."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/author"Hayashi H."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/author"Nakai Y."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/author"Nakai Y."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/author"Nakai M."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/author"Nakai M."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/pages"27469-27476"xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/pages"27469-27476"xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/title"Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/title"Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems."xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/volume"283"xsd:string
http://purl.uniprot.org/citations/18664566http://purl.uniprot.org/core/volume"283"xsd:string
http://purl.uniprot.org/citations/18664566http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18664566
http://purl.uniprot.org/citations/18664566http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18664566
http://purl.uniprot.org/citations/18664566http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18664566
http://purl.uniprot.org/citations/18664566http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18664566