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© Institut Pasteur
Cristaux de cellulase, enzyme purifiée de Clostridium thermocellum permettant la digestion de la cellulose. Image colorisée.
Publication : Molecular biotechnology

Characterisation of a DNA polymerase highly mutated along the template binding interface

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular biotechnology - 01 Sep 2010

Vichier-Guerre S, Jestin JL

Link to Pubmed [PMID] – 20407851

Mol. Biotechnol. 2010 Sep;46(1):58-62

Phage display establishes a link between a polypeptide and its corresponding gene. It has been much used for the isolation of proteins binding to chosen molecular targets. A second link was designed more recently between a phage-displayed enzyme and its reaction product. Affinity chromatography for the product then allows the isolation of catalytically active enzymes and of their genes. Using this strategy, a polymerase with 15 mutations was selected by directed evolution of Thermus aquaticus DNA polymerase I. The kinetic characterisation reported here highlights the variant’s broad template specificity and classifies this enzyme as a thermostable DNA-dependent and RNA-dependent DNA-polymerase.

http://www.ncbi.nlm.nih.gov/pubmed/20407851