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TATA-box binding protein (TBP) interactions with TBP-associated factors (TAFs) are required for the transcription of RNA polymerases. One particular TBP-TAF complex, snRNA-activating protein complex (SNAPC), is unusual in that it regulates basal transcription of both RNA polymerase II and III by binding specifically to a non-TATA-box proximal sequence element (PSE). SNAPC consists of five subunits of varying size. SNAPC binds to Oct-1 and TBP, which are activators of snRNA and RNA polymerases, respectively. The POU domain of Oct-1 binds to SNAPC 190 and effectively recruits SNAPC to the PSE. The cooperative binding of SNAPC and Oct-1 to their respective sequence elements is mediated by a nucleosome positioned between the two sequence elements. SNAPC 19 mediates the assembly of the subunits to form a functional SNAPC transcription regulator. SNAPC 50 (also designated PTFβ) contains two zinc finger motifs and binds to SNAPC 43 (also designated PTFγ) but not SNAPC 45 (PTFδ).
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