Protein & Peptide Letters

Author(s): R. Lavigne, B. Roucourt, K. Hertveldt and G. Volckaert

DOI: 10.2174/0929866054696127

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Characterization of the Bacteriophage ΦKMV DNA Ligase

Page: [645 - 648] Pages: 4

  • * (Excluding Mailing and Handling)

Abstract

Gene 17 product (gp17) of the Pseudomonas aeruginosa-infecting bacteriophage phiKMV shows in silico similarity to T7 DNA ligase. In a semi-quantitative activity assay, it is shown that gp17 is a functional, ATP-dependent DNA ligase, in spite of some structural differences related to DNA-binding properties). Enzymatic activity of His6-based purified expression product was optimised (4°C at 24h for sticky end double-stranded DNA fragments) and estimated at 0.5 Weiss U/μg.

Keywords: dna ligase, bacteriophage, recombinant protein, phikmv