The dissociation rate of a winged helix protein-DNA complex is influenced by non-DNA contact residues.
The dissociation constants and the half-lives of the DNA complexes of winged helix protein Genesis and its mutants were investigated. Our data show that substitutions of non-DNA contact residues in the two highly dynamic wing sequences dramatically change the off rates of the complexes. Thus, our data indicate that the off rate of a DNA complex is encoded in the amino acid sequence of the DNA-binding protein and/or should be a unique property for a protein-DNA complex. Our data also indicate that the local structural transition of a DNA-binding protein in its DNA recognition process is likely to go through a transition state, which can control the on and off rates of a complex.
Shiyanova
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Department of Biochemistry and Molecular Biology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois, 60612, USA.
Liao
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D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D001667:Binding, Competitive; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D051858:Forkhead Transcription Factors; D006207:Half-Life; D019077:Helix-Turn-Helix Motifs; D007700:Kinetics; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011392:Proline / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D051381:Rats; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013816:Thermodynamics