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Gene Review

tRNA-Glu  -  tRNA

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Disease relevance of tRNA-Glu

 

High impact information on tRNA-Glu

  • The competition strength of the tRNAPhe, tRNAMetf, and tRNAGlu promoters is 20-fold greater than that for the tRNAThrACN and tRNACys promoters [2].
  • The strengths of the promoters of the genes were ordered: tRNAMetf greater than tRNAPhe greater than 14 S rRNA greater than 21 S rRNA greater than tRNAGlu greater than Oli-1 much greater than tRNACys [3].
  • More surprisingly, extended sequence homologies were seen between the flanking regions of the pY 20 tRNA Glu 3 gene and a tRNA Ser gene [2,3] [4].
  • Moreover, at 0 degrees C, tRNAGlu strongly inhibits the binding of Phe-tRNA to poly(U)-programmed ribosomes via either the enzymic (EF-Tu-promoted) or nonenzymic pathway [5].
  • Addition of glutamic acid diamide induces an increase of the tRNAPhe.tRNAGlu pairing constant, which is however equivalent to that observed for tRNAPhe.tRNALys pairing and thus does not demonstrate a selective binding to tRNAGlu [6].
 

Chemical compound and disease context of tRNA-Glu

 

Biological context of tRNA-Glu

  • The same result was also obtained in the methylation of A19 (counting from the 3' end of the molecule) in tRNA1Val, tRNAPhe, tRNAfMet, tRNASer, and tRNAGlu individually and in the case of their mixing in pairs [8].
 

Associations of tRNA-Glu with chemical compounds

 

Physical interactions of tRNA-Glu

  • Selective binding of these amino acid residues to tRNAPhe is deduced from the observed concentration dependence which is not compatible with a corresponding binding process to tRNAGlu [6].

References

  1. 31P magnetic resonance of tRNA. Guéron, M., Shulman, R.G. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  2. In vitro transcription and promoter strength analysis of five mitochondrial tRNA promoters in yeast. Wettstein-Edwards, J., Ticho, B.S., Martin, N.C., Najarian, D., Getz, G.S. J. Biol. Chem. (1986) [Pubmed]
  3. Transcriptional regulation of the mitochondrial genome of yeast Saccharomyces cerevisiae. Mueller, D.M., Getz, G.S. J. Biol. Chem. (1986) [Pubmed]
  4. Structural comparison of two yeast tRNA Glu 3 genes. Eigel, A., Olah, J., Feldmann, H. Nucleic Acids Res. (1981) [Pubmed]
  5. Effect of transfer ribonucleic acid dimer formation on polyphenylalanine biosynthesis. Miller, D.L., Yamane, T., Hopfield, J.J. Biochemistry (1981) [Pubmed]
  6. Selective binding of amino acid residues to tRNA molecules detected by anticodon-anticodon interactions. Bujalowski, W., Porschke, D. Z. Naturforsch., C, J. Biosci. (1988) [Pubmed]
  7. Tertiary structure of tRNAs in solution monitored by phosphodiester modification with ethylnitrosourea. Vlassov, V.V., Giegé, R., Ebel, J.P. Eur. J. Biochem. (1981) [Pubmed]
  8. Use of the method of mixed substrates to study the specificity of tRNA methylases. Gambaryan, A.S., Venkstern, T.V., Baev, A.A. Mol. Biol. (Mosk.) (1976) [Pubmed]
 
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