Abstract
A conformational difference between the structure of tRNAPhe and Cbz-Phe-tRNAPhe from Escherichia coli was detected using the spin label method. A comparison of the respective rotational correlation time (tau c) values of three differently located spin labels, indicates that upon aminoacylation of tRNAPhe, the 4-thiouridine residue region and the miniloop region become more flexible, while the environment of the anticodon loop is not affected. These observations suggest that the main difference in structure between charged and uncharged tRNA resides in the release and exposure of the TpsiC loop for eventual binding to the ribosomes.
Highlights
A conformational difference between the structure of tRNAPhe and Cbz-Phe-tRNAPhe from Escherichia coli was detected using the spin label method
BSL-Phe-tRNAPhe was completely deacylated by treatment at 37” for 5 hours at pH 7.5 the resulting EPR spectrum was converted back to the spectrum of BSL-tRNAPhe
We can conclude that a conformational change in tRNAPhe is induced by the aminoacylation and is reversible
Summary
(Received for publication, October 8, 1975 and in revised form, December 1, 19751. From the DPpartement de Chimie, Universite CP. 6210, Montreal, H3C 3V1, Canada de Montrt?al, SUMMARY. A comparison of the respective rotational correlation time (7,) values of three differently located spin labels, indicates that upon aminoacylation of tRNAPhe, the 4-thiouridine residue region and the miniloop region become more flexible, while the environment of the anticodon loop is not affected. These observations suggest that the main difference in structure between charged and uncharged tRNA resides in the release and exposure of the T+C loop for eventual binding to the ribosomes. The experiments reported here describe the use of these spin labels to investigate changes in conformation that accompany aminoacylation of E. coli tRNAPhe
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