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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Analysis of ligation and DNA binding by Escherichia coli DNA ligase (LigA).

NAD(+)-dependent DNA ligases are essential enzymes in bacteria, with the most widely studied of this class of enzymes being LigA from Escherichia coli. NAD(+)-dependent DNA ligases comprise several discrete structural domains, including a BRCT domain at the C-terminus that is highly-conserved in this group of proteins. The over-expression and purification of various fragments of E. coli LigA allowed the investigation of the different domains in DNA-binding and ligation by this enzyme. Compared to the full-length protein, the deletion of the BRCT domain from LigA reduced in vitro ligation activity by 3-fold and also reduced DNA binding. 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. In gel-mobility shift experiments, the isolated BRCT domain bound DNA in a stable manner and to a wider range of DNA molecules compared to full LigA. Thus, the BRCT domain of E. coli LigA can bind DNA, but it is not essential for DNA nick-joining activity in vitro or in vivo.[1]

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]
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