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Gene Review

leuS  -  leucyl-tRNA synthetase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of leuS

  • Within the domain, we have identified a crucial 20-amino-acid peptide that confers editing capacity when transplanted into the inactive Escherichia coli LeuRS editing domain [1].
  • Evidence from sequence alignment and crystal structure of LeuRS from Thermus thermophilus shows that A293 was conserved as R (K) or A and is located at a small helix in the editing domain of the enzyme facing the active site [2].

High impact information on leuS


Biological context of leuS

  • It seems that the flexibility of the first base pair affects the editing reaction of LeuRS [8].
  • These recombinant plasmids were transformed or cotransformed into E. coli to produce five monomeric and five heterodimeric LeuRS mutants [9].
  • Here we report the isolation and characterization of three LeuRS mutants with point mutations at this position (T252Y, T252L, and T252F) [10].
  • These results suggest that the region around E292-A293 may be responsible for maintaining the proper conformation of LeuRS required for the tRNA charging activity [11].
  • However, the complete genome sequence of a hyper thermophile Aquifex aeolicus suggests that the gene for leucyl-tRNA synthetases (LeuRS) is probably split into two pieces (leuS and leuS') [12].

Associations of leuS with chemical compounds

  • It is possible that the yeast mitochondria have evolved to tolerate lower levels of fidelity in protein synthesis or have developed alternate mechanisms to enhance discrimination of leucine from non-cognate amino acids that can be misactivated by leucyl-tRNA synthetase [4].
  • However, mutated LeuRS can mischarge tRNA(Leu) isoacceptors tRN or tRN with isoleucine to different extents [8].
  • Leucyl-tRNA synthetase (LeuRS) relies on its editing function to correct misaminoacylation of tRNA(Leu) by isoleucine and methionine [10].
  • To achieve atomic level insight into the role of T252 in LeuRS and the editing reaction of aaRSs, a series of molecular modeling studies including homology modeling and automated docking simulations were carried out [13].

Other interactions of leuS

  • The argU gene helps A. aeolicus LeuRS, which contains AGA/AGG codons in exceptionally high frequency, express well in E. coli [14].

Analytical, diagnostic and therapeutic context of leuS

  • Although the E292-A293-cleaved LeuRS could not catalyze aminoacylation, fluorescence titration revealed that its tRNA binding ability was almost identical to that of wild-type LeuRS [11].
  • By using the genes encoding A. aeolicus and E. coli LeuRS as PCR templates, the genes encoding the alpha and beta subunits from A. aeolicus alphabeta-LeuRS and the equivalent amino- and carboxy-terminal parts of E. coli LeuRS (identified as alpha' and beta') were amplified and recombined using suitable plasmids [9].


  1. Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution. Zhao, M.W., Zhu, B., Hao, R., Xu, M.G., Eriani, G., Wang, E.D. EMBO J. (2005) [Pubmed]
  2. Effect of alanine-293 replacement on the activity, ATP binding, and editing of Escherichia coli leucyl-tRNA synthetase. Chen, J.F., Li, T., Wang, E.D., Wang, Y.L. Biochemistry (2001) [Pubmed]
  3. Sequence and structural similarities between the leucine-specific binding protein and leucyl-tRNA synthetase of Escherichia coli. Williamson, R.M., Oxender, D.L. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  4. A Viable Amino Acid Editing Activity in the Leucyl-tRNA Synthetase CP1-splicing Domain Is Not Required in the Yeast Mitochondria. Karkhanis, V.A., Boniecki, M.T., Poruri, K., Martinis, S.A. J. Biol. Chem. (2006) [Pubmed]
  5. Leucyl-tRNA synthetase consisting of two subunits from hyperthermophilic bacteria Aquifex aeolicus. Xu, M.G., Chen, J.F., Martin, F., Zhao, M.W., Eriani, G., Wang, E.D. J. Biol. Chem. (2002) [Pubmed]
  6. The molecular basis of leucine auxotrophy of quinone-treated Escherichia coli. Active site-directed modification of leucyl-tRNA synthetase by 6-amino-7-chloro-5,8-dioxoquinoline. Wiebauer, K., Ogilvie, A., Kersten, W. J. Biol. Chem. (1979) [Pubmed]
  7. ATP-analogues as substrates for the leucyl-tRNA synthetase from Escherichia coli MRE 600. Marutzky, R., Flossdorf, J., Kula, M.R. Nucleic Acids Res. (1976) [Pubmed]
  8. Discrimination of tRNA(Leu) isoacceptors by the mutants of Escherichia coli leucyl-tRNA synthetase in editing. Du, X., Wang, E.D. Biochemistry (2002) [Pubmed]
  9. Enzymes assembled from Aquifex aeolicus and Escherichia coli leucyl-tRNA synthetases. Zhao, M.W., Hao, R., Chen, J.F., Martin, F., Eriani, G., Wang, E.D. Biochemistry (2003) [Pubmed]
  10. Attenuation of the editing activity of the Escherichia coli leucyl-tRNA synthetase allows incorporation of novel amino acids into proteins in vivo. Tang, Y., Tirrell, D.A. Biochemistry (2002) [Pubmed]
  11. The peptide bond between E292-A293 of Escherichia coli leucyl-tRNA synthetase is essential for its activity. Li, T., Guo, N., Xia, X., Wang, E.D., Wang, Y.L. Biochemistry (1999) [Pubmed]
  12. Leucyl-tRNA synthetase from the extreme thermophile Aquifex aeolicus has a heterodimeric quaternary structure. Gouda, M., Yokogawa, T., Asahara, H., Nishikawa, K. FEBS Lett. (2002) [Pubmed]
  13. Molecular modeling study of the editing active site of Escherichia coli leucyl-tRNA synthetase: two amino acid binding sites in the editing domain. Lee, K.W., Briggs, J.M. Proteins (2004) [Pubmed]
  14. High-level expression and single-step purification of leucyl-tRNA synthetase from Aquifex aeolicus. Ling, C., Zheng, Y.G., Wang, E.D. Protein Expr. Purif. (2004) [Pubmed]
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