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Gene Review

ligA  -  DNA ligase, NAD(+)-dependent

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2406, JW2403, dnaL, lig, lop, ...
 
 
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Disease relevance of ligA

  • Using an E. coli strain harbouring a temperature-sensitive mutation of ligA, the over-expression of protein with its BRCT domain deleted enabled growth at the non-permissive temperature [1].
  • On the basis of the identification of this mechanism of action, we propose to change the name of the Mu lig gene (thought originally to be the structural gene for a bacteriophage ligase) to gem (gene expression modulation) [2].
 

High impact information on ligA

  • DNA sequence comparison of the ligA genes from wild type and temperature-sensitive S. aureus strain NT64 identified a single base alteration that is predicted to result in the amino acid substitution E46G [3].
  • The ligJ gene is transcribed in the same direction as ligABC genes and consists of an 1,023-bp open reading frame encoding a polypeptide with a molecular mass of 38,008 Da, which is located 73-bp upstream from ligA [4].
  • Protocatechuate 4,5-dioxygenase was efficiently expressed in Escherichia coli with the aid of the lac promoter, and the polypeptides of the ligA and ligB gene products were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and amino acid sequencing [5].
  • Thus, through this mechanism, the Mu lig gene product is able to modulate gene expression and hence suppress the effects of the E. coli ligts7 mutation [2].
  • We found that an E. coli ligts7 strain lysogenic for the Mu lig3 mutant shows: (i) an increment in the host DNA ligase activity; (ii) an increase in the specific mRNA of the host lig gene; (iii) an increase (towards the relaxed state) in the average linking number of a resident plasmid; and (iv) a reduction in DNA gyrase activity [2].
 

Chemical compound and disease context of ligA

  • There was an appreciable reduction in the survival of steroid treated polA and lig mutants of E. coli K12 compared to the wild type strain [6].
 

Biological context of ligA

 

Analytical, diagnostic and therapeutic context of ligA

  • Southern blot analysis indicated the conservation of the lig genes among pathogenic leptospires [8].

References

  1. Analysis of ligation and DNA binding by Escherichia coli DNA ligase (LigA). Wilkinson, A., Smith, A., Bullard, D., Lavesa-Curto, M., Sayer, H., Bonner, A., Hemmings, A., Bowater, R. Biochim. Biophys. Acta (2005) [Pubmed]
  2. Suppression of the thermosensitive DNA ligase mutations in Escherichia coli K12 through modulation of gene expression induced by phage Mu. Ghelardini, P., Liebart, J.C., Paolozzi, L., Pedrini, A.M. Mol. Gen. Genet. (1989) [Pubmed]
  3. Cloning and functional characterization of an NAD(+)-dependent DNA ligase from Staphylococcus aureus. Kaczmarek, F.S., Zaniewski, R.P., Gootz, T.D., Danley, D.E., Mansour, M.N., Griffor, M., Kamath, A.V., Cronan, M., Mueller, J., Sun, D., Martin, P.K., Benton, B., McDowell, L., Biek, D., Schmid, M.B. J. Bacteriol. (2001) [Pubmed]
  4. The 4-oxalomesaconate hydratase gene, involved in the protocatechuate 4,5-cleavage pathway, is essential to vanillate and syringate degradation in Sphingomonas paucimobilis SYK-6. Hara, H., Masai, E., Katayama, Y., Fukuda, M. J. Bacteriol. (2000) [Pubmed]
  5. Molecular cloning of the protocatechuate 4,5-dioxygenase genes of Pseudomonas paucimobilis. Noda, Y., Nishikawa, S., Shiozuka, K., Kadokura, H., Nakajima, H., Yoda, K., Katayama, Y., Morohoshi, N., Haraguchi, T., Yamasaki, M. J. Bacteriol. (1990) [Pubmed]
  6. Steroid induced single strand breaks in DNA mediated by active oxygen species and its biological consequences. Qadri, S.A., Ahmad, M. Biochem. Mol. Biol. Int. (1993) [Pubmed]
  7. Nucleotide sequence of the lig gene and primary structure of DNA ligase of Escherichia coli. Ishino, Y., Shinagawa, H., Makino, K., Tsunasawa, S., Sakiyama, F., Nakata, A. Mol. Gen. Genet. (1986) [Pubmed]
  8. Leptospiral immunoglobulin-like proteins elicit protective immunity. Koizumi, N., Watanabe, H. Vaccine (2004) [Pubmed]
 
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