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Effect of Protein Binding on Ultrafast DNA Dynamics: Characterization of a DNA:APE1 Complex
2005
Biophysical Journal
Synthetic oligonucleotides with a fluorescent coumarin group replacing a basepair have been used in recent time-resolved Stokes-shift experiments to measure DNA dynamics on the femtosecond to nanosecond timescales. Here, we show that the APE1 endonuclease cleaves such a modified oligonucleotide at the abasic site opposite the coumarin with only a fourfold reduction in rate. In addition, a noncatalytic mutant (D210N) binds tightly to the same oligonucleotide, albeit with an 85fold reduction in
doi:10.1529/biophysj.105.062695
pmid:16199493
pmcid:PMC1366978
fatcat:2nxpsbucqncfxbgdjrut57ywbe