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.
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