Disease relevance of lysS

• Lysyl-tRNA synthetases are synthesized from two distinct genes in Escherichia coli, lysS (constitutively) and lysU (inducibly); however, the physiological significance and the differential control mechanism of these two genes have been a long-standing puzzle [1].
• We report the cloning and complete nucleotide sequence of the Campylobacter jejuni lysyl-tRNA synthetase gene (lysS) [2].
• The gene encoding lysyl-tRNA synthetase (lysS) in Mycoplasma hominis was cloned and sequenced [3].
• The detection of an archaeal-type lysyl-tRNA synthetase in B. burgdorferi and other pathogenic spirochetes, but not to date elsewhere in bacteria or eukarya, indicates that the gene that encodes this enzyme has a common origin with its orthologue from the archaeal kingdom [4].
• Archaeal-type lysyl-tRNA synthetase in the Lyme disease spirochete Borrelia burgdorferi [4].

High impact information on lysS

• Heterologous expression of this open reading frame in Escherichia coli led to the production of a protein with canonical lysyl-tRNA synthetase activity in vitro [4].
• Lysyl-tRNA synthetase aminoacylates CoA-SH with lysine, leucine, threonine, alanine, valine, and isoleucine [5].
• Loss of this base pair reduces mischarging by the E. coli lysyl-tRNA synthetase [6].
• On the basis of the structure of L-lysine complexed with E. coli LysRS2 (lysS), residues implicated in amino acid recognition and discrimination were systematically replaced [7].
• Reverse transcription/polymerase chain reaction was used to demonstrate that this lysS gene is co-transcribed with gltX in R. meliloti [8].

Biological context of lysS

• The constitutive lysyl-tRNA synthetase gene (lysS) was mapped at 62.1 min on the Escherichia coli chromosome by a combination of conjugation and transduction, with physical confirmation by two-dimensional gel electrophoresis [9].
• The T. thermophilus lysS gene was overexpressed in Escherichia coli by placing it downstream of the E. coli beta-galactosidase gene promoter on plasmid pBluescript and by changing the ribosome-binding site [10].
• The lysS gene has been identified by a herC mutation which restores maintenance of the mutant ColE1 replicon [11].
• These results contrast with the situation encountered in Escherichia coli where lysyl-tRNA synthetase is coded by two distinct genes, lysS and lysU, and further address the possible biological significance of this gene duplication [12].
• Using random Tn10 insertion mutagenesis, we isolated an Escherichia coli mutant strain affected in the regulation of lysU, the gene encoding the inducible form of lysyl-tRNA synthetase [13].

Associations of lysS with chemical compounds

• The properties of the two lysine transport systems, of the lysyl-tRNA synthetase and of the aspartokinase III (AK III) were studied in the mutant and in the parent strain [14].
• No difference between the two strains was evidenced as regards 1) the affinity of the transport systems for lysine and thialysine 2) the activity of the lysyl-tRNA synthetase 3) the allosteric inhibition of the AK III by lysine and thialysine [14].
• By varying time and the concentrations of lysine, Mg(2+), or LysRS, the adenylation of Hint was found to be dependent on the formation of lysyl-AMP [15].

References