Nucleotide sequence, heterologous expression and novel purification of DNA ligase from Bacillus stearothermophilus

James A. Brannigan, Stephen R. Ashford, Aidan J. Doherty, David J. Timson, Dale B. Wigley

Research output: Contribution to journalArticlepeer-review

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. Copyright (C) 1999 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)413-418
Number of pages6
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1432
Issue number2
DOIs
Publication statusPublished - 13 Jul 1999

Keywords

  • Bacillus stearothermophilus
  • DNA ligation
  • DNA replication
  • NAD
  • Thermostable protein

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