ArticleMethods in molecular biology (Clifton, N.J.)2014
Engineering and flow-cytometric analysis of chimeric LAGLIDADG homing endonucleases from homologous I-OnuI-family enzymes.
Article in Methods in molecular biology (Clifton, N.J.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Optimization of Protein Thermostability and Exploitation of Recognition Behavior to Engineer Altered Protein-DNA Recognition.Structure (London, England : 1993) · 2020Article
- Engineering altered protein-DNA recognition specificity.Nucleic acids research · 2018Review
- Crystallographic analyses illustrate significant plasticity and efficient recoding of meganuclease target specificity.Nucleic acids research · 2017Article
- Tuning DNA binding affinity and cleavage specificity of an engineered gene-targeting nuclease via surface display, flow cytometry and cellular analyses.Protein engineering, design & selection : PEDS · 2017Article
- The Structural Basis of Asymmetry in DNA Binding and Cleavage as Exhibited by the I-SmaMI LAGLIDADG Meganuclease.Journal of molecular biology · 2016Article
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Authors and funding
3 authors.
Funding
Abstract
LAGLIDADG homing endonucleases (LHEs) are valuable tools for genome engineering, and our ability to alter LHE target site specificity is rapidly evolving. However, widespread use of these enzymes is limited due to the small number of available engineering scaffolds, each requiring extensive redesign to target widely varying DNA sequences. Here, we describe a technique for the chimerization of homologous I-OnuI family LHEs. Chimerization greatly expands the pool of unique starting scaffolds, thereby enabling more effective and efficient LHE redesign. I-OnuI family enzymes are divided into N- and C-terminal halves based on sequence alignments, and then combinatorially rejoined with a hybrid linker. The resulting chimeric enzymes are expressed on the surface of yeast where stability, DNA binding affinity, and cleavage activity can be assayed by flow cytometry.
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