| Description |
Zinc-finger proteins are one of the most common regulatory factors in eukaryotes. One subclass of these proteins has the recently described BED finger DNA-binding domain, characterized by the signature Cx2CxnHx3?C5[H/C] (xn is a variable spacer) and the presence of two highly conserved aromatic amino acids (tryptophan and phenylalanine) at its N terminus. BED finger proteins are thought to function as either transcription activators or repressors by modifying local chromatin structure on binding to GC-rich sequences.
Reference:
1. L. Aravind, The BED finger, a novel DNA-binding domain in chromatin-boundary-element-binding proteins and transposases. Trends Biochem Sci 25, 421 (2000).
2. M. Saghizadeh, N. B. Akhmedov, C. K. Yamashita, Y. Gribanova, V. Theendakara, E. Mendoza, S. F. Nelson, A. V. Ljubimov, D. B. Farber, ZBED4, a BED-type zinc-finger protein in the cones of the human retina. Invest Ophthalmol Vis Sci 50, 3580 (2009).
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