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Nucleic Acids Research, 1978, Vol. 5, No. 5 1551-1560
© 1978

Articles

A novel conformational change of the anticodon region of tRNAPhe (yeast)

Claus Urbanke and Guenter Maass

Institut für Klinische Biochemie und Physiologische Chemie, Abteilung Biophysikalische Chemie, Medizinische Hochschule Hannover Karl-Wiechert-Allee 9, D-3000 Hannover 61, GFR

Received January 27, 1978. The temperature dependence of the fluorescence of the Y-base of tRNAPhe (yeast) was investigated kinetically by the temperature jump method. In the range between –15 °C and +30 °C a novel conformational transition of the tRNA could be characterized. This conformational change was found in the absence of any artificial label; it is a characteristic property of tRNAPhe in its native structure. This transition accounts for 30 % of the total fluorescence change. Its activation enthalpy is 16 kcal/mole (67 kJ/mole), and the transition enthalpy is between –2 kcal/mole and +2 kcal/mole (±8 kJ/mole). A model is represented in which this transition can be explained by a a change in the stacking pattern of the anticodon loop. The experimental findings are discussed with respect to several hypotheses about the molecular mechanism of protein biosynthesis which postulate conformational rearrangements of the anticodon loop.


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