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Free-energy dissipation constrainst on the accuracy of enzymatic selections

Published online by Cambridge University Press:  17 March 2009

C. Blomberg ,
M. Ehrenberg  and
C. G. Kurland
C. Blomberg
Affiliation:
Research Group for Theoretical Biophysics, Royal Institute of Technology, S–100 44 Stockholm
M. Ehrenberg
Affiliation:
Department of Medical Biophysics, Karolinska Institutet, S–104 or Stockholm
C. G. Kurland
Affiliation:
Institute of Molecular Biology, Uppsala Universitet, S–751 22 Uppsala
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Extract

A bacterium incorporates amino acids into protein with an error frequency close to one in three thousand (Edelman & Gallant, 1977). Nevertheless, the structural differences between related amino acids are so small that it is difficult to see how they can be distinguished from each other with such accuracy (see, for example, Pauling, 1958).

Indeed, the selection of amino acids during protein synthesis is carried out twice: first by the aminoacyl-tRNA synthetases and then by the codon-programmed ribosome. Each of these substrate selections is in fact a double selection. In the case of the synthetase both a particular amino acid and a corresponding cognate tRNA must be chosen to form the aminoacyl-tRNA. On the ribosome, the aminoacyl-tRNA must be matched with a cognate codon, and then the mRNA must be advanced by exactly one codon length to position the next codon in the appropriate ribosome site so that it too can be translated.

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 13 , Issue 2 , May 1980 , pp. 231 - 254
Copyright
Copyright © Cambridge University Press 1980

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References

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