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http://purl.uniprot.org/citations/18538672 | http://www.w3.org/2000/01/rdf-schema#comment | "Methanothermobacter thermautotrophicus contains a multi-aminoacyl-tRNA synthetase complex (MSC) of LysRS, LeuRS and ProRS. Elongation factor (EF) 1A also associates to the MSC, with LeuRS possibly acting as a core protein. Analysis of the MSC revealed that LysRS and ProRS specifically interact with the idiosyncratic N- and C-termini of LeuRS, respectively. EF-1A instead interacts with the inserted CP1 proofreading domain, consistent with models for post-transfer editing by class I synthetases such as LeuRS. Together with previous genetic data, these findings show that LeuRS plays a central role in mediating interactions within the archaeal MSC by acting as a core scaffolding protein."xsd:string |
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http://purl.uniprot.org/citations/18538672 | http://purl.uniprot.org/core/author | "Ibba M."xsd:string |
http://purl.uniprot.org/citations/18538672 | http://purl.uniprot.org/core/author | "Hausmann C.D."xsd:string |
http://purl.uniprot.org/citations/18538672 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18538672 | http://purl.uniprot.org/core/name | "FEBS Lett"xsd:string |
http://purl.uniprot.org/citations/18538672 | http://purl.uniprot.org/core/pages | "2178-2182"xsd:string |
http://purl.uniprot.org/citations/18538672 | http://purl.uniprot.org/core/title | "Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex."xsd:string |
http://purl.uniprot.org/citations/18538672 | http://purl.uniprot.org/core/volume | "582"xsd:string |
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