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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

tRNA-Asp  -  tRNA

Thermus thermophilus HB8

 
 
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Disease relevance of tRNA-Asp

  • A stepwise mutational analysis of a minihelix derived from tRNA Sec in which sequence elements of tRNA Asp were introduced showed that the sequence of the amino acid- acceptor branch of Escherichia coli tRNA Sec contains a specific structural element that hinders its binding to T.thermophilus EF-Tu-GTP [1].
 

High impact information on tRNA-Asp

  • Transplantation of these elements in tRNAAsp and tRNAPhe converts specificity toward glycine albeit conservation of nucleotide 73 [2].
  • Kinetic investigations show that the two enzymes are specific for aspartic acid activation and tRNAAsp charging. tRNA aspartylation by the thermostable AspRSs is governed by thermodynamic parameters which values are similar to those measured for mesophilic aspartylation systems [3].
  • We demonstrate here, using RNA variants derived from tRNAAsp, that the minimalist aminoacylated structure able to interact efficiently with elongation factor Tu comprises a 10 base-pair helix linked to the 3'-terminal NCCA sequence [4].
 

Analytical, diagnostic and therapeutic context of tRNA-Asp

  • The function of this C7.G66/G49.U65/C50.G64 box was tested by its transplantation into a minihelix derived from tRNA Asp, abolishing its recognition by EF-Tu-GTP [1].

References

  1. Antideterminants present in minihelix(Sec) hinder its recognition by prokaryotic elongation factor Tu. Rudinger, J., Hillenbrandt, R., Sprinzl, M., Giegé, R. EMBO J. (1996) [Pubmed]
  2. tRNA glycylation system from Thermus thermophilus. tRNAGly identity and functional interrelation with the glycylation systems from other phylae. Mazauric, M.H., Roy, H., Kern, D. Biochemistry (1999) [Pubmed]
  3. Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Structural and biochemical properties of the two enzymes. Becker, H.D., Reinbolt, J., Kreutzer, R., Giegé, R., Kern, D. Biochemistry (1997) [Pubmed]
  4. Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu. Rudinger, J., Blechschmidt, B., Ribeiro, S., Sprinzl, M. Biochemistry (1994) [Pubmed]
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