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A transcriptional activator is a protein (transcription factor) that increases transcription of a gene or set of genes. [1] Activators are considered to have positive control over gene expression, as they function to promote gene transcription and, in some cases, are required for the transcription of genes to occur.
The transactivation domain or trans-activating domain (TAD) is a transcription factor scaffold domain which contains binding sites for other proteins such as transcription coregulators. These binding sites are frequently referred to as activation functions (AFs). [1] TADs are named after their amino acid composition.
Illustration of an activator. In molecular biology, a transcription factor (TF) (or sequence-specific DNA-binding factor) is a protein that controls the rate of transcription of genetic information from DNA to messenger RNA, by binding to a specific DNA sequence.
A coactivator is a type of transcriptional coregulator that binds to an activator (a transcription factor) to increase the rate of transcription of a gene or set of genes. [1] The activator contains a DNA binding domain that binds either to a DNA promoter site or a specific DNA regulatory sequence called an enhancer.
A transcription factor is a protein that binds to specific DNA sequences (enhancer or promoter), either alone or with other proteins in a complex, to control the rate of transcription of genetic information from DNA to messenger RNA by promoting (serving as an activator) or blocking (serving as a repressor) the recruitment of RNA polymerase.
Transactivation can be triggered either by endogenous cellular or viral proteins, also called transactivators. These protein factors act in trans (i.e., intermolecularly). HIV and HTLV are just two of the many viruses that encode transactivators to enhance viral gene expression.
It is required for the successful transcription of nearly all class II gene promoters in yeast. [7] It works in the same manner in mammals. The mediator functions as a coactivator and binds to the C-terminal domain of RNA polymerase II holoenzyme, acting as a bridge between this enzyme and transcription factors. [8]
All seven STAT proteins share a common structural motif consisting of an N-terminal domain followed by a coiled-coil, DNA-binding domain, linker, Src homology 2 (SH2), and a C-terminal transactivation domain. Much research has focused on elucidating the roles each of these domains play in regulating different STAT isoforms.