Open AccessDNA flexibility variation may dominate DNase I cleavage.
Author(s) -
Michael E. Hogan,
Mark W. Roberson,
Robert H. Austin
Publication year - 1989
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.23.9273
Subject(s) - dna , cleavage (geology) , flexibility (engineering) , rigidity (electromagnetism) , repressor , stiffness , biophysics , genetics , physics , materials science , biology , mathematics , gene , thermodynamics , composite material , statistics , fracture (geology) , transcription factor
In a previous experimental study, we proposed that the bending and torsional stiffness of DNA display a systematic sequence dependence. Subsequently, we developed an elastic strain model to quantify the sequence dependence of the bending and torsional rigidity in terms of nearest neighbor interactions and used that model to analyze the sequence dependence of the 434 repressor binding to its operator. The analysis presented here shows that, in the absence of significant local variation of DNA secondary structure, DNase I cleavage is strongly correlated with local variation in the bending flexibility as calculated from our elastic strain model and that the agreement is also quantitatively significant. It is proposed that analysis using elastic strain models will provide a preliminary set of biochemical and chemical tools to explore the relation between DNA flexibility and the binding of other proteins.