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Nucleic Acids Research, 1981, Vol. 9, No. 4 1031-1044
© 1981

MOLECULAR BIOLOGY

Conformational states of yeast tRNAPhe in the complex with congnate and non cognate synthetases

Rudolf Rigler$, Lennart Nilsson$,§, Wolfgang Wintermeyer{dagger}, Ulrich Pachmann{dagger},* and Hans G. Zachau{dagger}

$Department of Medical Biophysics, Karolinska Institute Stockholm §Department of Theoretcial Physics, Royal Institute of Technology Stockholm, Sweden {dagger}Institut für physiologische Chemie, Physikalische Biochemie und Zellbiologie, Universität München München, GFR

Received September 16, 1980.

The influence of phenylalanyl-tRNA synthetase and seryl-tRNA synthetase on the conformation and structural kinetics of yeast tRNAPhe was investigated. Ethidium substituted for dihydrouracil at position 16 or 17 was used as a structural probe, showing the existence of three conformational states in tRNA. The dis tribution of states (T1, T2, T3) is changed only by the cognate synthetase towards T3 which probably is related to the X-ray structure. The binding of phenylalanyl-tRNA synthetase leads to an about 10-fold increase in the fast transition T1 {rightleftharpoons} T2 which has been assigned to changes in the anticodon loop conformation and to a 2-3 fold increase in the slow transition which probably extends to other parts of the tRNA molecule. The observed rates for the transition T2 {rightleftharpoons} T3 are close to that observed for the transfer of the activated phenylalanine to tRNAPhe. This raises the possibility that the conformational transition in tRNA is the rate limiting step in the charging reaction.

* present address: Krankenhaus seefeld, Hauptstr.33, D-8031 Seefeld, FRG.


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