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Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy | Nature Structural & Molecular Biology
Description:
Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa-tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, at a resolution of ∼9 Å, showing that during the incorporation of the aa-tRNA into the 70S ribosome of Escherichia coli, the flexibility of aa-tRNA allows the initial codon recognition and its accommodation into the ribosomal A site. In addition, a conformational change observed in the GTPase-associated center (GAC) of the ribosomal 50S subunit may provide the mechanism by which the ribosome promotes a relative movement of the aa-tRNA with respect to EF-Tu. This relative rearrangement seems to facilitate codon recognition by the incoming aa-tRNA, and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu. From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome.
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nature portfolio permissions reprints privacy policy elongation factor ef-tu-gdp advertising codon-anticodon recognition-dependent signal danish research council swedish research council social media strategic research health research nature 365 nature 389 nature 407 nature 334 nature 250 nature personal data author correspondence elongation factor ef-tu mutation glycine-222→aspartic acid data protection springerlink instant access codon-dependent conformational change accommodated a-site trna codon-recognition complex permissions article valle elongation factor tu trigger gtp hydrolysis facilitate codon recognition protein synthesis kinetics cryo-em reveals molecular dynamics simulations building protein models initial codon recognition l11-rna complex molecular biology cryo-electron microscopy privacy guanine exchange factor elongation factors tu posttermination ribosomal complex competing financial interests phenylalanine transfer rna codon-anticodon interaction stalled ternary complex yeast phenylananine trna joachim frank issue learn
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- Is there proofreading during polypeptide synthesis?
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headline:Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy
description:Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa-tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, at a resolution of â¼9 Ã
, showing that during the incorporation of the aa-tRNA into the 70S ribosome of Escherichia coli, the flexibility of aa-tRNA allows the initial codon recognition and its accommodation into the ribosomal A site. In addition, a conformational change observed in the GTPase-associated center (GAC) of the ribosomal 50S subunit may provide the mechanism by which the ribosome promotes a relative movement of the aa-tRNA with respect to EF-Tu. This relative rearrangement seems to facilitate codon recognition by the incoming aa-tRNA, and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu. From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome.
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headline:Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy
description:Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa-tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, at a resolution of â¼9 Ã
, showing that during the incorporation of the aa-tRNA into the 70S ribosome of Escherichia coli, the flexibility of aa-tRNA allows the initial codon recognition and its accommodation into the ribosomal A site. In addition, a conformational change observed in the GTPase-associated center (GAC) of the ribosomal 50S subunit may provide the mechanism by which the ribosome promotes a relative movement of the aa-tRNA with respect to EF-Tu. This relative rearrangement seems to facilitate codon recognition by the incoming aa-tRNA, and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu. From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome.
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- pdns6.ultradns.co.uk
CDN Services {📦}
- Crossref