title: The T box regulatory element controlling expression of the class I lysyl-tRNA synthetase of Bacillus cereus strain 14579 is functional and can be partially induced by reduced charging of asparaginyl-tRNAAsn.
abstract: BACKGROUND
  Lysyl-tRNA synthetase (LysRS) is unique within the aminoacyl-tRNA synthetase family in that both class I (LysRS1) and class II (LysRS2) enzymes exist. LysRS1 enzymes are found in Archaebacteria and some eubacteria while all other organisms have LysRS2 enzymes. All sequenced strains of Bacillus cereus (except AH820) and Bacillus thuringiensis however encode both a class I and a class II LysRS. The lysK gene (encoding LysRS1) of B. cereus strain 14579 has an associated T box element, the first reported instance of potential T box control of LysRS expression.
  
  
  RESULTS
  A global study of 891 completely sequenced bacterial genomes identified T box elements associated with control of LysRS expression in only four bacterial species: B. cereus, B. thuringiensis, Symbiobacterium thermophilum and Clostridium beijerinckii. Here we investigate the T box element found in the regulatory region of the lysK gene in B. cereus strain 14579. We show that this T box element is functional, responding in a canonical manner to an increased level of uncharged tRNALys but, unusually, also responding to an increased level of uncharged tRNAAsn. We also show that B. subtilis strains with T box regulated expression of the endogenous lysS or the heterologous lysK genes are viable.
  
  
  CONCLUSIONS
  The T box element controlling lysK (encoding LysRS1) expression in B. cereus strain 14579 is functional, but unusually responds to depletion of charged tRNALys and tRNAAsn. This may have the advantage of making LysRS1 expression responsive to a wider range of nutritional stresses. The viability of B. subtilis strains with a single LysRS1 or LysRS2, whose expression is controlled by this T box element, makes the rarity of the occurrence of such control of LysRS expression puzzling.
authors.affiliation: Smurfit Institute of Genetics, Trinity College Dublin, Dublin, Ireland. kdevine@tcd.ie
authors.forename: Niall
authors.initials: N
authors.lastname: Foy
authors.forename: Brian
authors.initials: B
authors.lastname: Jester
authors.forename: Gavin C
authors.initials: GC
authors.lastname: Conant
authors.forename: Kevin M
authors.initials: KM
authors.lastname: Devine
mesh_terms: D000595:Amino Acid Sequence; D001409:Bacillus cereus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D015971:Gene Expression Regulation, Enzymologic; D008250:Lysine-tRNA Ligase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D012348:RNA, Transfer, Asn / Q000378:metabolism*; D050436:Regulatory Elements, Transcriptional; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D012346:RNA, Transfer, Amino Acyl; D012348:RNA, Transfer, Asn; D008250:Lysine-tRNA Ligase