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Gene Review

lysS  -  lysyl-tRNA synthetase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of lysS

  • In Escherichia coli, lysyl-tRNA synthetase activity is encoded by either a constitutive lysS gene or an inducible one, lysU [1].
  • However, the capacity of tRNA(3)(Lys) to interact with lysyl-tRNA synthetase does not entirely explain the enhanced preference for selection of tRNA(3)(Lys) for the replication of HIV-1 [2].

High impact information on lysS

  • Loss of this base pair reduces mischarging by the E. coli lysyl-tRNA synthetase [3].
  • This cold sensitivity was suppressed by a multi-copy plasmid carrying lysU, the inducible gene [4].
  • These data are interpreted as indicating that lysS is functionally replaceable by lysU for cell growth, and that the cold sensitivity of lysS1 is caused by insufficient expression of lysU at low temperatures [4].
  • Here, we show that the N-terminal domains of three E. coli multidomain proteins such as lysyl-tRNA synthetase, threonyl-tRNA synthetase, and aconitase are potent solubility enhancers for various C-terminal heterologous proteins [5].
  • Transformation of the mutant strain with a plasmid, pK8, containing the metK coding sequence and promoter region as a 1.8-kilobase insert into pBR322 restored normal induction of C14.7 and G13.5, but did not prevent constitutive expression of the lysU gene product in the medium required for growth of this strain [6].

Biological context of lysS


Analytical, diagnostic and therapeutic context of lysS

  • To demonstrate an association between LysRS induction and two distinct LysRS genes, Southern blotting was performed with a probe representing an 871-bp fragment amplified from an internal portion of the coding region of the lysU gene [8].


  1. Comparison of the enzymatic properties of the two Escherichia coli lysyl-tRNA synthetase species. Brevet, A., Chen, J., Lévêque, F., Blanquet, S., Plateau, P. J. Biol. Chem. (1995) [Pubmed]
  2. Complementation of Human Immunodeficiency Virus Type 1 Replication by Intracellular Selection of Escherichia coli Formula Supplied in trans. McCulley, A., Morrow, C.D. J. Virol. (2006) [Pubmed]
  3. Design of a bacterial host for site-specific incorporation of p-bromophenylalanine into recombinant proteins. Kwon, I., Wang, P., Tirrell, D.A. J. Am. Chem. Soc. (2006) [Pubmed]
  4. Differential regulation of two genes encoding lysyl-tRNA synthetases in Escherichia coli: lysU-constitutive mutations compensate for a lysS null mutation. Kawakami, K., Ito, K., Nakamura, Y. Mol. Microbiol. (1992) [Pubmed]
  5. N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers. Kim, C.W., Han, K.S., Ryu, K.S., Kim, B.H., Kim, K.H., Choi, S.I., Seong, B.L. Protein Sci. (2007) [Pubmed]
  6. Abnormal induction of heat shock proteins in an Escherichia coli mutant deficient in adenosylmethionine synthetase activity. Matthews, R.G., Neidhardt, F.C. J. Bacteriol. (1988) [Pubmed]
  7. Characterization of a Mycoplasma hominis gene encoding lysyl-tRNA synthetase (LysRS). Ozkökmen, D., Birkelund, S., Christiansen, G. FEMS Microbiol. Lett. (1994) [Pubmed]
  8. The occurrence of duplicate lysyl-tRNA synthetase gene homologs in Escherichia coli and other procaryotes. Saluta, M.V., Hirshfield, I.N. J. Bacteriol. (1995) [Pubmed]
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