Function of Y in codon-anticodon interaction of tRNA Phe |
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Authors: | O Pongs E Reinwald |
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Institution: | Max-Planck-Institut für Molekulare Genetik 1 Berlin 33 (Dahlem), Ihnestrasse 63-73, Germany |
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Abstract: | Molar association constants of binding oligonucleotides to the anticodon loops of (yeast) tRNAPhe, (yeast) tRNAHClPhe and (E. coli) tRNAFMet have been determined by equilibrium dialysis. From the temperature dependence of the molar association constants, ΔF, ΔH and ΔS of oligomer-anticodon loop interaction have been determined. The data indicate that the free energy change of codon-anticodon interaction is highly influenced by the presence of a modified purine (tRNAPhe), of an unmodified purine (tRNAFMet) or its absence (tRNAHClPhe). Excision of the modified purine Y in the anticodon loop of tRNAPhe results in a conformational change of the anticodon loop, which is discussed on the basis of the corresponding changes in ΔF, ΔH and ΔS. |
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