S. Bushmeyer et al., CHARACTERIZATION OF FUNCTIONAL DOMAINS WITHIN THE MULTIFUNCTIONAL TRANSCRIPTION FACTOR, YY1, The Journal of biological chemistry, 270(50), 1995, pp. 30213-30220
YY1 is a multifunctional transcription factor capable of either activa
tion or repression of transcription. Using a series of mutant proteins
, we have characterized domains responsible for activation or repressi
on. We found that the YY1 transcriptional activation domain lies near
the amino terminus and requires amino acids 16-29 and 80-100 for maxim
al activity. The region between residues 16 and 29 has the potential t
o form an acidic amphipathic helix, whereas residues between 80 and 10
0 are rich in proline and glutamine. The YY1 repression domain lies ne
ar the carboxyl terminus and is embedded within the YY1 zinc finger re
gion necessary for binding to DNA. Deletion of YY1 amino acids, which
include zinc fingers 3 and 4, abolishes repression. However, site-dire
cted mutagenesis, progressive deletion, and internal deletion mutant a
nalyses indicate that the normal structures of zinc fingers 3 and 4 ar
e not required for repression.