Characterization of the Bacteriophage ΦKMV DNA Ligase

R.      Lavigne; B.      Roucourt; K.      Hertveldt; G.      Volckaert

doi:10.2174/0929866054696127

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

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Protein & Peptide Letters

Title: Characterization of the Bacteriophage ΦKMV DNA Ligase

Volume: 12 Issue: 7

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

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Keywords: dna ligase, bacteriophage, recombinant protein, phikmv

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.

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Lavigne R., Roucourt B., Hertveldt K. and Volckaert G., Characterization of the Bacteriophage ΦKMV DNA Ligase, Protein & Peptide Letters 2005; 12 (7) . https://dx.doi.org/10.2174/0929866054696127