Nucleic Acids Research, Vol 24, Issue 14 2640-2647, Copyright © 1996 by Oxford University Press
R Arnold, M Burcin, B Kaiser, M Muller and R Renkawitz
NeP1 binds to the F1 silencer element of the chicken lysozyme gene and, in
the presence of TR, v-ERBA or RAR, synergistically represses
transcriptional activity. This repression involves a silencing mechanism
acting independently of the relative promoter position. Here we show that
NeP1 alone can induce a significant directed bend on DNA. The chicken
homologue of human NeP1, CTCF, shows identical binding and bending
properties. In contrast, the isolated DNA binding domain of CTCF
efficiently binds DNA, but fails to confer bending. Similarly, the TR-RXR
hetero- or homodimer, binding adjacent to NeP1 at the F2 sequence, do not
show significant DNA bending. The binding of the T3 ligand to TR changes
neither the magnitude nor the direction of the NeP1 induced bend. However,
when all factors are bound simultaneously as a quaternary complex, the
TR-RXR heterodimer changes the location of the bend center, the flexure
angle and the bending direction.
ARTICLES
DNA bending by the silencer protein NeP1 is modulated by TR and RXR
Genetisches Institut, Justus-Liebig-Universitat, Giessen, Germany.
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