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- W2124538608 abstract "Experimental analysis and manipulation of protein-DNA interactions pose unique biophysical challenges arising from the structural and chemical homogeneity of DNA polymers. We report the use of yeast surface display for analytical and selection-based applications for the interaction between a LAGLIDADG homing endonuclease and its DNA target. Quantitative flow cytometry using oligonucleotide substrates facilitated a complete profiling of specificity, both for DNA-binding and catalysis, with single base pair resolution. These analyses revealed a comprehensive segregation of binding specificity and affinity to one half of the pseudo-dimeric interaction, while the entire interface contributed specificity at the level of catalysis. A single round of targeted mutagenesis with tandem affinity and catalytic selection steps provided mechanistic insights to the origins of binding and catalytic specificity. These methods represent a dynamic new approach for interrogating specificity in protein-DNA interactions." @default.
- W2124538608 created "2016-06-24" @default.
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- W2124538608 date "2009-09-08" @default.
- W2124538608 modified "2023-10-01" @default.
- W2124538608 title "High-resolution profiling of homing endonuclease binding and catalytic specificity using yeast surface display" @default.
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- W2124538608 doi "https://doi.org/10.1093/nar/gkp726" @default.
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