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http://purl.uniprot.org/citations/20584901http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20584901http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20584901http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/20584901http://www.w3.org/2000/01/rdf-schema#comment"Bacterial and eukaryotic transfer RNAs have been shown to contain hypermodified adenosine, 2-methylthio-N(6)-threonylcarbamoyladenosine, at position 37 (A(37)) adjacent to the 3'-end of the anticodon, which is essential for efficient and highly accurate protein translation by the ribosome. Using a combination of bioinformatic sequence analysis and in vivo assay coupled to HPLC/MS technique, we have identified, from distinct sequence signatures, two methylthiotransferase (MTTase) subfamilies, designated as MtaB in bacterial cells and e-MtaB in eukaryotic and archaeal cells. Both subfamilies are responsible for the transformation of N(6)-threonylcarbamoyladenosine into 2-methylthio-N(6)-threonylcarbamoyladenosine. Recently, a variant within the human CDKAL1 gene belonging to the e-MtaB subfamily was shown to predispose for type 2 diabetes. CDKAL1 is thus the first eukaryotic MTTase identified so far. Using purified preparations of Bacillus subtilis MtaB (YqeV), a CDKAL1 bacterial homolog, we demonstrate that YqeV/CDKAL1 enzymes, as the previously studied MTTases MiaB and RimO, contain two [4Fe-4S] clusters. This work lays the foundation for elucidating the function of CDKAL1."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.106831"xsd:string
http://purl.uniprot.org/citations/20584901http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.106831"xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Atta M."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Atta M."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Fontecave M."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Fontecave M."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Forouhar F."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Forouhar F."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Hunt J.F."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Hunt J.F."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Douki T."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Douki T."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Arragain S."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Arragain S."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Mulliez E."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Mulliez E."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Tomizawa K."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Tomizawa K."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Handelman S.K."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Handelman S.K."xsd:string
http://purl.uniprot.org/citations/20584901http://purl.uniprot.org/core/author"Wei F.Y."xsd:string