Abstract
AS a part of our research on the structure–function relationships of tRNAvalI we have been mapping the regions that take part in the recognition of valyl tRNA ligase. Using the “dissected molecule” method1, we have shown that associated molecules consisting of tRNAValI fragments lacking nucleotides in the anticodon loop, the dihydrouridine loop (D) or the thymidine loop (T) retain their acceptor activity. By contrast, dissected molecules devoid of the pentanucleotide A36CACGp (the sequence A36C belongs to the anticodon T35AC) or lacking any quarter (F1–19, F17–35 or F36–57) are inactive2–4. Here we report a study of the acceptor activity of other incomplete tRNAvalI molecules. The principal inference is that the dinucleotides A36Cp in the anticodon loop and 5′-terminal pG1Gp in the CCA stem are at least parts of two different recognition sites of this tRNA.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
We are sorry, but there is no personal subscription option available for your country.
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Bayev, A. A., Fodor, I., Mirzabekov, A. D., Axelrod, V. D., and Kazarinova, L. Ya., Mol. Biol., 1, 859 (1967).
Mirzabekov, A. D., Kazarinova, L. Ya., and Bayev, A. A., Mol. Biol., 3, 879 (1969).
Mirzabekov, A. D., Kazarinova, L. Ya., Lastity, D., and Bayev, A. A., FEBS Letters, 3, 268 (1969).
Mirzabekov, A. D., Lastity, D., and Bayev, A. A., FEBS Lett., 4, 281 (1969).
Mirzabekov, A. D., Lastity, D., Levina, E. S., and Bayev, A. A., FEBS Letters, 7, 95 (1970).
Beardsley, K., and Cantor, C. R., Proc. US Nat. Acad. Sci., 65, 39 (1970).
Bayev, A. A., Venkstern, T. V., Mirzabekov, A. D., Krutilina, A. I., Li, L., and Axelrod, V. D., Mol. Biol., 1, 754 (1967).
Yaniv, M., and Barrell, B. G., Nature, 222, 278 (1969).
Lagerkvist, U., and Waldenstrom, J., J. Mol. Biol., 8, 28 (1964).
Schulman, L. H., and Chambers, R. W., Proc. US Nat. Acad. Sci., 61, 308 (1968).
Takemura, S., Kawata, M., Hashimoto, S., and Murakami, M., Proc. Seventh Intern. Symp. Chem. Natural Products, Riga, B4, 193, Riga (1970).
Seno, T., Kobayashi, I., Fukuhara, M., and Nashimura, S., FEBS Lett., 7, 343 (1970).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
MIRZABEKOV, A., LASTITY, D., LEVINA, E. et al. Localization of Two Recognition Sites in Yeast Valine tRNA I. Nature New Biology 229, 21–22 (1971). https://doi.org/10.1038/newbio229021a0
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1038/newbio229021a0
This article is cited by
-
The early history of tRNA recognition by aminoacyl-tRNA synthetases
Journal of Biosciences (2006)
-
Origin of the genetic code and specificity of tRNA aminoacylation. A testable model
Origins of Life (1984)
-
Amino Acid Acceptor Stem of E. coli Suppressor tRNATyr is a Site of Synthetase Recognition
Nature New Biology (1973)