A Yeast-Based Recombination Assay for Homing Endonuclease Activity View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2014

AUTHORS

Jean-Charles Epinat

ABSTRACT

Homing endonucleases (HEs) are natural enzymes that cleave long DNA target with a high specificity and trigger homologous recombination at the exact site of the break. Such mechanisms can thus be used for all the applications covered today by the generic name of "genome engineering": targeted sequence insertion, removal, or editing. However, before being able to address those applications, the engineering of HEs must be mastered so that any potential target would be efficiently and specifically recognized and cleaved. Working on the I-CreI model, we have developed a very powerful platform to generate HEs with new tailored specificity. We have put in place the first in vivo, functional, high throughput assay to generate I-CreI variants and measure their activity. We use semi-rational design combined with proprietary in silico predictions to design and synthesize I-CreI mutants that are tested for their capacity to induce homologous recombination in a yeast cell. The process has been standardized and robotized so that we can generate thousands of I-CreI derivatives, characterize their cleavage profile, and deliver them for further applications in the research, therapeutic, or agrobusiness fields. More... »

PAGES

105-26

References to SciGraph publications

  • 1997-05. The first genome from the third domain of life in NATURE
  • 2013. Engineered Meganucleases for Genome Engineering Purposes in SITE-DIRECTED INSERTION OF TRANSGENES
  • 2008. Triplex-Mediated Gene Modification in CHROMOSOMAL MUTAGENESIS
  • 2013. Bio-applications Derived from Site-Directed Genome Modification Technologies in SITE-DIRECTED INSERTION OF TRANSGENES
  • 2013. Engineered Zinc Finger Nucleases for Targeted Genome Editing in SITE-DIRECTED INSERTION OF TRANSGENES
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    http://scigraph.springernature.com/pub.10.1007/978-1-62703-968-0_9

    DOI

    http://dx.doi.org/10.1007/978-1-62703-968-0_9

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/24510264


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