Nuclear import and DNA-binding activity of RFX1. Evidence for an autoinhibitory mechanism.

@article{KatanKhaykovich2001NuclearIA,
  title={Nuclear import and DNA-binding activity of RFX1. Evidence for an autoinhibitory mechanism.},
  author={Yael Katan-Khaykovich and Yosef Shaul},
  journal={European journal of biochemistry},
  year={2001},
  volume={268 10},
  pages={
          3108-16
        }
}
RFX1 binds and regulates the enhancers of a number of viruses and cellular genes. RFX1 belongs to the evolutionarily conserved RFX protein family that shares a DNA-binding domain and a conserved C-terminal region. In RFX1 this conserved region mediates dimerization, and is followed by a unique C-terminal tail, containing a highly acidic stretch. In HL-60 cells nuclear translocation of RFX1 is regulated by protein kinase C with unknown mechanisms. By confocal fluorescence microscopy, we have… 
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