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Transcription activators are proteins that are responsible for allowing RNA polymerase to initiate transcription. They have two essential domains- one that binds to DNA and another one that activates transcription.
The DNA-binding domains contain one of several characteristic structural motifs, including common motifs like the helix-turn-helix, zinc finger, and leucine zipper structures.
A helix-turn-helix domain is made up of two alpha helices joined together by an amino-acid chain that represents the turn. One helix is responsible for recognizing the DNA sequence and fits into the major groove. These proteins bind to DNA as dimers.
A zinc finger contains an alpha helix and a two-strand beta sheet held together by a zinc atom. The helix binds to the major groove with the help of two histidines in its amino acid chain.
A leucine zipper is made up of two monomers that interact with each other in the shape of a Y that binds to the DNA. The monomers consist of leucine at every seventh position at the C-terminal end which interacts with the leucine on the opposite monomer. The N-terminal of the monomer which is made up of basic motifs binds to the DNA.
The other essential domain in
Transcription activators are proteins that promote the transcription of genes from DNA to RNA. In most cases, these proteins contain two separate doma…
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