Structural elements defining elongation factor Tu mediated suppression of codon ambiguity
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چکیده
منابع مشابه
Structural elements defining elongation factor Tu mediated suppression of codon ambiguity
In most prokaryotes Asn-tRNA(Asn) and Gln-tRNA(Gln) are formed by amidation of aspartate and glutamate mischarged onto tRNA(Asn) and tRNA(Gln), respectively. Coexistence in the organism of mischarged Asp-tRNA(Asn) and Glu-tRNA(Gln) and the homologous Asn-tRNA(Asn) and Gln-tRNA(Gln) does not, however, lead to erroneous incorporation of Asp and Glu into proteins, since EF-Tu discriminates the mis...
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The mechanisms by which elongation factor Tu (EF-Tu) promotes the binding of aminoacyl-tRNA to the A site of the ribosome and, in particular, how GTP hydrolysis by EF-Tu is triggered on the ribosome, are not understood. We report steady-state and time-resolved fluorescence measurements, performed in the Escherichia coli system, in which the interaction of the complex EF-Tu.GTP.Phe-tRNAPhe with ...
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Elongation factor (EF) Tu promotes the binding of aminoacyl-tRNA (aa-tRNA) to the acceptor site of the ribosome. This process requires the formation of a ternary complex (EF-Tu.GTP.aa-tRNA). EF-Tu is released from the ribosome as an EF-Tu.GDP complex. Exchange of GDP for GTP is carried out through the formation of a complex with EF-Ts (EF-Tu.Ts). Mammalian mitochondrial EF-Tu (EF-Tu(mt)) differ...
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Kirromycin, also known as mccimycin, is a member of the elfamycin family of antibiotics. These antibiotics inhibit bacterial protein synthesis by binding tightly to elongation factor Tu (Emu) a 43.2 kD G-protein. E m u .GTP is able to carry aminoacyl tRNA to the ribosome in the presence of kirromycin in the usual way, but after hydrolysis of GTP EFTu.GDP is unable to leave the ribosome. Consequ...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2007
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/gkm211