Effect of modification of tRNA nucleotide 37 on the tRNA interaction with the A and P sites of the Escherichia coli 70S ribosome

Autor: A. L. Konevega, A. V. Peshekhonov, N. G. Soboleva, Makhno Vi, V.I. Katunin
Rok vydání: 2006
Předmět:
Zdroj: Molecular Biology. 40:597-610
ISSN: 1608-3245
0026-8933
DOI: 10.1134/s0026893306040121
Popis: The modified nucleotide 3′ of the tRNA anticodon is an important structural element that regulates the codon-anticodon interaction in the ribosome by stacking with codon-anticodon bases. The presence and identity (pyrimidine, purine, or modified purine) of this nucleotide significantly affects the energy of stacking in the A and P sites of the ribosome. Modification of nucleotide 37 does not contribute to stacking in the A site of the 70S ribosome, while its effect is substantial in the P site. The enthalpies of tRNA interactions with the A and P sites in the ribosome are similar and considerably lower than the enthalpy of the interactions of two tRNAs with the cognate anticodons in solution, suggesting that the ribosome contributes to the enthalpy-related portion of the free energy of tRNA binding by directly forming additional interactions with tRNA or by indirectly stabilizing the conformation of the codon-anticodon complex. In addition to stacking, tRNA binding in the A and P sites is further stabilized by interactions that involve magnesium ions. The number of ions involved in the formation of the tRNA-ribosome complex depends on the identity of tRNA nucleotide 37.
Databáze: OpenAIRE
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