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Papers In Press, published online ahead of print November 27, 2001
Cell Biology, Memorial Sloan-Kettering Cancer Center, New York, NY 10021
Corresponding Author: r-benezra{at}ski.mskcc.org
Homodimeric complexes of members of the E protein family of bHLH transcription factors are important for tissue specific activation of genes in B lymphocytes[1-4]. These homodimers, however, have little activity on myogenic enhancers[5]. We report here the identification of a novel cis-acting transcriptional repression domain in the E protein family of bHLH transcription factors. This domain, the Rep domain, is present in each of the known vertebrate E proteins. Extensive mapping analysis demonstrates that this domain is an acidic region of 30 amino acids with a predicted loop structure. Fusion studies indicate that the Rep domain can repress both of the E protein transactivation domains (AD1 and AD2). Physiologically, the Rep domain plays a key role in maintaining E protein homodimers in an inactive state on myogenic enhancers. In addition, we demonstrate that Rep domain mediated repression of AD1 is a necessary for the function of MyoD/E protein heterodimeric complexes. These studies demonstrate that the Rep domain is important for modulating the transcriptional activity of E proteins and provide key insights into both the selectivity and mechanism of action of E protein containing bHLH protein complexes.
J. Biol. Chem, 10.1074/jbc.M110659200
Submitted on November 6, 2001
Revised on November 26, 2001
Accepted on November 27, 2001
Enhancer specific modulation of E protein activity
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