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Mol. Cell. Biol., 08 1997, 4696-4706, Vol 17, No. 8
ST Neuteboom and C Murre
We have used a binding site selection strategy to determine the optimal
binding sites for Pbx proteins by themselves and as heterodimeric partners
with various Hox gene products. Among the Pbx proteins by themselves, only
Pbx3 binds with high affinity, as a monomer or as a homodimer, to an
optimal binding site, TGATTGATTTGAT. An inhibitory domain located N
terminal of the Pbx1 homeodomain prevents intrinsic Pbx1 binding to this
sequence. When complexed with Hoxc-6, each of the Pbx gene products binds
the same consensus sequence, TGATTTAT, which differs from the site bound by
Pbx3 alone. Three members of the Antennapedia family, Hoxc-6, Hoxb-7, and
Hoxb-8, select the same binding site in conjunction with Pbx1. The
affinities of these proteins as heterodimeric partners with Pbx1 for the
selected optimal binding site are similar. However, the binding specificity
of Hox proteins for optimal binding sites is increased, compared to
nonspecific DNA, in the presence of Pbx proteins. Thus, while cooperative
DNA binding involving heterodimers of Pbx and Hox gene products derived
from members within the Antennapedia family does not increase binding site
selectivity, DNA binding specificity of the Hox gene products is
significantly enhanced in the presence of Pbx.
Copyright © 1997, American Society for Microbiology
Pbx raises the DNA binding specificity but not the selectivity of antennapedia Hox proteins
Department of Biology, University of California, San Diego, La Jolla 92093, USA.
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