PMID: 41223Nov 24, 1979

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

Nucleic Acids Research
P Wrede, A Rich

Abstract

Initiator tRNAs have an anticodon loop conformation distinct from that of elongation tRNAs as detected by susceptibility to S1 nuclease. We now find the anticodon loop conformation of E. coli tRNAfMet to be stable under different salt conditions as detected by using S1 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.

References

Oct 1, 1990·International Journal of Biological Macromolecules·A JoachimiakT Mashkova
Apr 4, 1997·Journal of Molecular Biology·D C Schweisguth, P B Moore
Jun 1, 1982·European Journal of Biochemistry·K S Aultman, S H Chang

Citations

Oct 17, 1978·Biochemistry·R M WurstA M Maxam
Mar 8, 1979·Nature·R W SchevitzJ L Sussman
Jul 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·P WredeA Rich
Aug 1, 1977·Nucleic Acids Research·H Donis-KellerW Gilbert
Jan 1, 1979·Nucleic Acids Research·D H GaussM Sprinzl
Jan 1, 1969·Cold Spring Harbor Symposia on Quantitative Biology·S K DubeK A Marcker

Related Concepts

RNA Conformation
Alkalescens-Dispar Group
MT-TA gene
Triplet Codon-amino Acid Adaptor Activity
Macromolecular Alteration
N-Formylmethionine
Cytokinesis of the Fertilized Ovum
Transfer RNA
Spermine
Nuclease

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