| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10873958 | FEBS Letters | 2005 | 5 Pages |
Abstract
Aminoacyl-tRNA (aa-tRNA) is delivered to the ribosome in a ternary complex with elongation factor Tu (EF-Tu) and GTP. The stepwise movement of aa-tRNA from EF-Tu into the ribosomal A site entails a number of intermediates. The ribosome recognizes aa-tRNA through shape discrimination of the codon-anticodon duplex and regulates the rates of GTP hydrolysis by EF-Tu and aa-tRNA accommodation in the A site by an induced fit mechanism. Recent results of kinetic measurements, ribosome crystallography, single molecule FRET measurements, and cryo-electron microscopy suggest the mechanism of tRNA recognition and selection.
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Authors
Marina V. Rodnina, Kirill B. Gromadski, Ute Kothe, Hans-Joachim Wieden,