Characterization of the Bacteriophage ΦKMV DNA Ligase

Authors: Lavigne, R.; Roucourt, B.; Hertveldt, K.; Volckaert, G.

Source: Protein and Peptide Letters, Volume 12, Number 7, October 2005 , pp. 645-648(4)

Publisher: Bentham Science Publishers

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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: bacteriophage; dna ligase; phikmv; recombinant protein

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866054696127

Affiliations: Laboratory of Gene Technology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21, Leuven, B-3001, Belgium;

Publication date: October 1, 2005

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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