  We present a theoretical model of facilitated diffusion of proteins in the
cell nucleus. This model, which takes into account the successive
binding/unbinding events of proteins to DNA, relies on a fractal description of
the chromatin which has been recently evidenced experimentally. Facilitated
diffusion is shown quantitatively to be favorable for a fast localization of a
target locus by a transcription factor, and even to enable the minimization of
the search time by tuning the affinity of the transcription factor with DNA.
This study shows the robustness of the facilitated diffusion mechanism, invoked
so far only for linear conformations of DNA.
