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J Biol Chem. 2004 Nov 19;279(47):49281-8. Epub 2004 Sep 17.

The nuclear receptor co-repressor (N-CoR) utilizes repression domains I and III for interaction and co-repression with ETO.

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Laboratory of Molecular Biophysics, The Rockefeller University, New York, New York 10021, USA.


The acute human leukemias are associated with the presence of chimeric gene products that arise from spontaneous chromosomal translocations. The t(8;21) translocation gene product led to the discovery of the Eight Twenty-One (ETO) gene. When fused to RUNX1, ETO is thought to mediate the formation of a repressive complex at RUNX1-dependent genes. ETO has also been found to act as a co-repressor of the promyelocytic zinc finger and Bcl-6 oncoproteins, suggesting that it may play a common role as a transcriptional co-repressor leading to human disease. An analysis of ETO-mediated repression revealed that one of the key binding partners of ETO is the nuclear receptor co-repressor (N-CoR). It is shown that two highly conserved domains of ETO interact with repression domains I and III of N-CoR. One of the ETO domains displays significant homology to Drosophila TAF(II)110, whereas the other is a predicted zinc binding motif that engages a conserved PPLXP motif in repression domain III of N-CoR. Together, these domains of ETO cooperate in repression with N-CoR and the binding sites in N-CoR overlap with those for other repressive factors. Thus, ETO has the potential to participate in a number of repressive complexes, which can be distinguished by their binding partners and target genes.

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