Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. TFIID, a transcription factor, coordinates these activities and binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. It is TBP, the TATA-binding protein. A distinctive feature of TBP is a long string of glutamines in the N-terminus. This region of the protein modulates the DNA binding activity of the C terminus, and modulation of DNA binding affects the rate of transcription complex formation and initiation of transcription. TFIID is associated with spinocerebellar ataxia 17, a neurodegenerative disorder classified as a polyglutamine disease (1).
Related Pathway
Wnt Signaling Pathway
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