Literature DB >> 10407164

Nucleotide sequence, heterologous expression and novel purification of DNA ligase from Bacillus stearothermophilus(1).

J A Brannigan1, S R Ashford, A J Doherty, D J Timson, D B Wigley.   

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.

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Year:  1999        PMID: 10407164     DOI: 10.1016/s0167-4838(99)00122-3

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  A DNA ligase from a hyperthermophilic archaeon with unique cofactor specificity.

Authors:  M Nakatani; S Ezaki; H Atomi; T Imanaka
Journal:  J Bacteriol       Date:  2000-11       Impact factor: 3.490

2.  Enzymes used in molecular biology: a useful guide.

Authors:  Laure Rittié; Bernard Perbal
Journal:  J Cell Commun Signal       Date:  2008-09-03       Impact factor: 5.782

3.  Adenylation-dependent conformation and unfolding pathways of the NAD+-dependent DNA ligase from the thermophile Thermus scotoductus.

Authors:  Daphné Georlette; Vinciane Blaise; Fabrice Bouillenne; Benjamin Damien; Sigridur H Thorbjarnardóttir; Eric Depiereux; Charles Gerday; Vladimir N Uversky; Georges Feller
Journal:  Biophys J       Date:  2004-02       Impact factor: 4.033

  3 in total

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