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Nucleotide sequence, heterologous expression and novel purification of DNA ligase from Bacillus stearothermophilus(1)
J A Brannigan1, S R Ashford, A J Doherty
1Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Biochimica Et Biophysica Acta
|July 17, 1999
Abstract:
The gene for DNA ligase (EC 6.5.1.2) from thermophilic bacterium Bacillus stearothermophilus NCA1503 has been cloned and the complete nucleotide sequence determined. The ligase gene encodes a protein 670 amino acids in length. The gene was overexpressed in Escherichia coli and the enzyme has been purified to homogeneity. Preliminary characterisation confirms that it is a thermostable, NAD(+)-dependent DNA ligase.