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Papers In Press, published online ahead of print May 4, 2000
Department of Microbiology, New York University School of Medicine, New York, NY 10016
Corresponding Author: basilc01{at}mcrcr.med.nyu.edu
The FGF-4 gene enhancer is synergistically activated by a ternary complex, Oct-3*, composed of Sox2 and Oct-3. The DNA binding- HMG- and POU-domains mediate cooperative assembly of Oct-3* on FGF enhancer DNA but are not sufficient to activate transcription. Deletion analysis of Oct-3 identified two activation domains, AD1 and AD2, that contribute to Oct-3* function. AD1, but not AD2, can also activate transcription in the absence of Sox2. Similar analysis of Sox2 identified three activation domains: R1 and R2 can potentiate weak activation by Sox2 in the absence of Oct-3 but are dispensible for Oct-3* function. Conversely, R3 function is only observed within Oct-3*. Analysis of Oct-1/Oct-3 chimeras additionally indicates that the Oct-3 homeodomain specifically modulates activation domain function within Oct-3*. Our results suggest that: 1) Cooperative DNA binding, mediated by the HMG- and POU- domains, stably tethers each factor to the enhancer, increasing the activity of intrinsic activation domains within each protein; 2) further protein-protein and protein-DNA interactions then lead to activation of latent activation domains. These findings may define a general mechanism for gene activation by Sox-POU complexes.
J. Biol. Chem, 10.1074/jbc.M000932200
Submitted on February 3, 2000
Revised on April 14, 2000
Accepted on May 4, 2000
Modulation of the activity of multiple transcriptional activation domains by the HMG and POU domains mediates the synergistic action of Sox2 and Oct-3 on the FGF-4 enhancer
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