| http://purl.uniprot.org/citations/15339930 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15339930 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15339930 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/15339930 | http://www.w3.org/2000/01/rdf-schema#comment | "The last biosynthetic step for 2-methylthio-N(6)-isopentenyl-adenosine (ms(2)i(6)A), present at position 37 in some tRNAs, consists of the methylthiolation of the isopentenyl-adenosine (i(6)A) precursor. In this work we have reconstituted in vitro the conversion of i(6)A to ms(2)i(6)A within a tRNA substrate using the iron-sulfur MiaB protein, S-adenosylmethionine (AdoMet), and a reducing agent. We show that a synthetic i(6)A-containing RNA corresponding to the anticodon stem loop of tRNA(Phe) is also a substrate. This study demonstrates that MiaB protein is a bifunctional system, involved in both thiolation and methylation of i(6)A. In this process, one molecule of AdoMet is converted to 5'-deoxyadenosine, probably through reductive cleavage and intermediate formation ofa5'-deoxyadenosyl radical as observed in other "Radical-AdoMet" enzymes, and a second molecule of AdoMet is used as a methyl donor as shown by labeling experiments. The origin of the sulfur atom is discussed."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m408562200"xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m408562200"xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/author | "Atta M."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/author | "Atta M."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/author | "Fontecave M."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/author | "Fontecave M."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/author | "Douki T."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/author | "Douki T."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/author | "Pierrel F."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/author | "Pierrel F."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/pages | "47555-47563"xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/pages | "47555-47563"xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/title | "MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/title | "MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA."xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15339930 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15339930 |