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In most cases, the transcription factors in eukaryotes which bind to promoter or enhancer sequences are activator proteins which induce transcription. That proteins generally have at least two distinct domains of protein structure, a DNA- binding domain which identify the specific DNA sequence to bind to and an activation domain responsible for bringing about the transcriptional activation by interaction with other transcription factors and the RNA polymerase molecule. Various transcription factors operate as dimers, either homodimers (identical subunits) or heterodimers (dissimilar subunits) with the subunits held together through dimerization domains. The DNA dimerization domains and binding domains have characteristic protein structures (motifs) which are explained
Figure: Looping out of DNA permitting the interaction of enhancer-bound factor(s) with the transcription initiation complex.
below. At last, some transcription factors example for steroid hormone receptors are responsive to specific short molecules (ligands) that regulate the activity of the transcription factor. In these cases, the ligand binds at a ligand-binding domain.
Why can it be said that the enzymatic action is highly specific? The enzymatic action is highly specific because only exact substrates of one enzyme bind to the activation cent
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