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Nucleic Acids Research, 1979, Vol. 7, No. 6 1457-1467
© 1979

Articles

Stability of the unique anticodon loop conformation of E.coli tRNAfMet

Paul Wrede and Alexander Rich

Department of Biology, Massachusetts Institute of Technology Cambridge, MA 02139, USA

Received August 29, 1979. Initiator tRNAs have an anticodon loop conformation distinct from that of elongation tRNAs as detected by susceptibility to SI nuclease. We now find the anticodon loop conformation of E.ooli tRNAMet to be stable under different salt conditions as detected by using SI nuclease as a structural probe. In contrast, a conformational change is observed in the T- and D- loop of this tRNA in the absence of added Mg2+. This change can be suppressed by spermine. Even under those conditions effecting a change in T- and D- loop conformation, the anticodon loop does not change. This suggests that the conformational shift is controlled by Mg2+ and restricted to the D- and T- loop region only without affecting the anticodon domain.

The use of S1 nuclease as a conformational probe requires the use of kinetic studies to determine the initial cleavage sites. Thus, the use of a strong inhibitor which immediately stops the action of this nuclease is necessary. ATP is shown to be such an inhibitor.


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P. Barraud, E. Schmitt, Y. Mechulam, F. Dardel, and C. Tisne
A unique conformation of the anticodon stem-loop is associated with the capacity of tRNAfMet to initiate protein synthesis
Nucleic Acids Res., September 1, 2008; 36(15): 4894 - 4901.
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