Nonspecific binding of lac repressor to DNA. II. A small-angle neutron-scattering study.
Complexes between lac repressor and DNA fragments from mononucleosomes have been studied by small-angle neutron scattering. Both the radius of gyration and the molecular weight of the complexes were measured, and the experimental results were interpreted according to a model with two types of complex (M. Charlier and J.-C. Maurizot, Biophys. Chem. 18 (1983) 303), and a statistical distribution of repressor on the DNA fragments. Good agreement between the model calculations and the experimental results was obtained. We concluded that there was an absence of strong cooperativity and of network formation between the complexes. The second type of binding, which does not induce any spectroscopic change, is marked by an increase in molecular weight of the complexes. Kinetic measurements were also made, which allowed the determination of the lifetime of the nonspecific DNA-repressor complexes.
D004247:DNA / Q000378:metabolism*; D004926:Escherichia coli; D007700:Kinetics; D009502:Neutrons; D009707:Nucleosomes; D011485:Protein Binding; D012097:Repressor Proteins / Q000378:metabolism*; D012542:Scattering, Radiation; D014157:Transcription Factors / Q000378:metabolism*
D009707:Nucleosomes; D012097:Repressor Proteins; D014157:Transcription Factors; D004247:DNA