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http://purl.uniprot.org/citations/11882645http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11882645http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11882645http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11882645http://www.w3.org/2000/01/rdf-schema#comment"The product of the miaB gene, MiaB, from Escherichia coli participates in the methylthiolation of the adenosine 37 residue during modification of tRNAs that read codons beginning with uridine. A His-tagged version of MiaB has been overproduced and purified to homogeneity. Gel electrophoresis and size exclusion chromatography revealed that MiaB protein is a monomer. As isolated MiaB contains both iron and sulfide and an apoprotein form can chelate as much as 2.5-3 iron and 3-3.5 sulfur atoms per polypeptide chain. UV-visible and EPR spectroscopy of MiaB indicate the presence of a [4Fe-4S] cluster under reducing and anaerobic conditions, whereas [2Fe-2S] and [3Fe-4S] forms are generated under aerobic conditions. Preliminary site-directed mutagenesis studies suggest that Cys(157), Cys(161), and Cys(164) are involved in iron chelation and that the cluster is essential for activity. Together with the previously shown requirement of S-adenosylmethionine (AdoMet) for the methylthiolation reaction, the finding that MiaB is an iron-sulfur protein suggests that it belongs to a superfamily of enzymes that uses [Fe-S] centers and AdoMet to initiate radical catalysis. MiaB is the first and only tRNA modification enzyme known to contain an Fe-S cluster."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c100609200"xsd:string
http://purl.uniprot.org/citations/11882645http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c100609200"xsd:string
http://purl.uniprot.org/citations/11882645http://purl.org/dc/terms/identifier"doi:10.1074/jbc.C100609200"xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/author"Atta M."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/author"Atta M."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/author"Fontecave M."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/author"Fontecave M."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/author"Pierrel F."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/author"Pierrel F."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/author"Bjoerk G.R."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/author"Bjoerk G.R."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/author"Bjork G.R."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/pages"13367-13370"xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/pages"13367-13370"xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/title"Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/title"Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein."xsd:string
http://purl.uniprot.org/citations/11882645http://purl.uniprot.org/core/volume"277"xsd:string