The ribosome translates the genetic information of an mRNA molecule into a sequence of amino acids. The ribosome utilizes tRNAs to connect elements of the RNA and protein worlds during protein synthesis, i.e. an anticodon as a unit of genetic information with the corresponding amino acid as a building unit of proteins. Three tRNA-binding sites are located on the ribosome, termed the A, P and E sites. In recent years the tRNA-binding sites have been localized on the ribosome by three different techniques, small-angle neutron scattering, cryo-electron microscopy and X-ray analyses of 70 S crystals. These high-resolution glimpses into various ribosomal states together with a large body of biochemical data reveal an intricate interplay between the tRNAs and the three ribosomal binding sites, providing an explanation for the remarkable features of the ribosome, such as the ability to select the correct ternary complex aminoacyl-tRNA · EF-Tu · GTP out of more than 40 extremely similar tRNA complexes, the precise movement of the tRNA2 · mRNA complex during translocation and the maintenance of the reading frame.
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Conference Article|
April 01 2002
Functions and interplay of the tRNA-binding sites of the ribosome
V. Márquez;
V. Márquez
1Max-Planck-Institut für Molekulare Genetik, AG Ribosomen, Ihnestrasse 73, D-14195 Berlin, Germany
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D. N. Wilson;
D. N. Wilson
1Max-Planck-Institut für Molekulare Genetik, AG Ribosomen, Ihnestrasse 73, D-14195 Berlin, Germany
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K. H. Nierhaus
K. H. Nierhaus
1
1Max-Planck-Institut für Molekulare Genetik, AG Ribosomen, Ihnestrasse 73, D-14195 Berlin, Germany
1To whom correspondence should be addressed (e-mail nierhaus@molgen.mpg.de).
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Publisher: Portland Press Ltd
Received:
November 22 2001
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2002 Biochemical Society
2002
Biochem Soc Trans (2002) 30 (2): 133–140.
Article history
Received:
November 22 2001
Citation
V. Márquez, D. N. Wilson, K. H. Nierhaus; Functions and interplay of the tRNA-binding sites of the ribosome. Biochem Soc Trans 1 April 2002; 30 (2): 133–140. doi: https://doi.org/10.1042/bst0300133
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