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Gene Review

lgt  -  phosphatidylglycerol-prolipoprotein...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2824, JW2796, umpA
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Disease relevance of lgt

  • Using E. coli strains containing varying levels of prolipoprotein diacylglyceryl modification activities due to mutations in or overexpression of the gene involved in diacylglyceryl modification (lgt), we have shown that the activities based on the peptide assay correlated well with the prolipoprotein-based assay [1].
  • Using a combination of biochemical, physical, and genetic techniques, we have shown that the umpA gene of Escherichia coli is allelic with the lgt (phosphatidylglycerol:prolipoprotein diacylglyceryl transferase) of Salmonella typhimurium [2].
  • A clone containing the gene for LGT, lgt, of the gram-positive species Staphylococcus aureus was isolated by complementation of the temperature-sensitive lgt mutant of E. coli (strain SK634) defective in LGT activity [3].
  • A Deltalgt (Lgt, lipoprotein diacylglyceryl transferase) isogenic mutant was obtained which indicates that lgt is not essential for cell growth in vitro, like in the Gram-positive bacterium Bacillus subtilis, but unlike in the proteobacteria Escherichia coli and Salmonella typhimurium [4].

High impact information on lgt

  • This open reading frame is immediately 5' to the thyA gene and is allelic to umpA of Escherichia coli [5].
  • These results suggest that the cloned gene encodes prolipoprotein glyceryl transferase (lgt), and in the wild-type background, this prolipoprotein modification enzyme is essential for the growth and viability of S. typhimurium [5].
  • The higher transcriptional level of all three genes at the preinfection time point indicates that only live and metabolically active rickettsiae are capable of infection and inducing host cell phagocytosis. lspA and lgt, which are involved in lipoprotein processing, show similar levels of expression [6].
  • One of these clones, pCUTFS2, also increased the copper tolerance of cutA, -C, and -E mutants, as well as that of a lipoprotein diacylglyceryl transferase (lgt) mutant of E. coli [7].
  • In E. coli, lgt and thyA (thymidylate synthase) form an operon [2].

Regulatory relationships of lgt


Analytical, diagnostic and therapeutic context of lgt

  • Three independent lgt mutant alleles from E. coli SK634, SK635, and SK636 and one lgt allele from S. typhimurium SE5221, all defective in LGT activity at the nonpermissive temperature, were cloned by PCR and sequenced [3].


  1. Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. Sankaran, K., Wu, H.C. J. Biol. Chem. (1994) [Pubmed]
  2. The umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling. Gan, K., Sankaran, K., Williams, M.G., Aldea, M., Rudd, K.E., Kushner, S.R., Wu, H.C. J. Bacteriol. (1995) [Pubmed]
  3. Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions. Qi, H.Y., Sankaran, K., Gan, K., Wu, H.C. J. Bacteriol. (1995) [Pubmed]
  4. Lipid modification of prelipoproteins is dispensable for growth in vitro but essential for virulence in Streptococcus pneumoniae. Petit, C.M., Brown, J.R., Ingraham, K., Bryant, A.P., Holmes, D.J. FEMS Microbiol. Lett. (2001) [Pubmed]
  5. Isolation and characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in prolipoprotein modification. Gan, K., Gupta, S.D., Sankaran, K., Schmid, M.B., Wu, H.C. J. Biol. Chem. (1993) [Pubmed]
  6. The lspA Gene, Encoding the Type II Signal Peptidase of Rickettsia typhi: Transcriptional and Functional Analysis. Rahman, M.S., Ceraul, S.M., Dreher-Lesnick, S.M., Beier, M.S., Azad, A.F. J. Bacteriol. (2007) [Pubmed]
  7. A Salmonella typhimurium genetic locus which confers copper tolerance on copper-sensitive mutants of Escherichia coli. Gupta, S.D., Wu, H.C., Rick, P.D. J. Bacteriol. (1997) [Pubmed]
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