词条 | TBP-associated factor |
释义 |
| Symbol = TAF | Name = TBP associated factor (TAF6) | image = PDB 1taf EBI.jpg | caption = drosophila dtafii42/dtafii62 (like TAF6/TAF9) heterotetramer, HFD | Pfam = PF02969 | Pfam_clan = CL0012 | InterPro = IPR004823 | PROSITE = | MEROPS = | SCOP = 1bh9 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} The TBP-associated factors (TAF) are proteins that associate with the TATA-binding protein in transcription initiation. It is a part of the transcription initiation factor TFIID multimeric protein complex. It also makes up many other factors, including SL1. They mediate the formation of the transcription preinitiation complex, a step preceeding transcription of DNA to RNA by RNA polymerase II. TAFs have a signature N-terminal histone-like fold domain (HFD).[1] This domain is implicated in the pairwise interaction among specific TAFs.[1] FunctionTFIIDTFIID plays a central role in mediating promoter responses to various activators and repressors. It binds tightly to TAFII-250 and directly interacts with TAFII-40. TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFS).[2] TAF is part of the TFIID complex, and interacts with the following:
Due to such interactions, they contribute transcription activation and to promoter selectivity.[2] Some pairs of TAF interact with each other to form "lobes" in TFIID. Pairs known or suggested to exist in TFIID include TAF6-TAF9, TAF4-TAF12, TAF11-13, TAF8-TAF10 and TAF3-TAF10.[1] SL1Selective factor 1 is composed of the TATA-binding protein and three TAF (TATA box-binding protein-associated factor) subunits (TAF1A, TAF1B, and TAF1C). These TAFs don't have a histone-like fold domain.[3]Other complexes{{missing information|section|subunits of SAGA and related complexes, and pair-forming therein|date=April 2019}}TAF is a part of SAGA (SPT-ADA-GCN5 acetylase) and related coactivation complexes.[1] Such complexes acetylate histone tails to activate genes.[4] Human has three SAGA-like complexes: PCAF, TFTC (TBP-free TAF-containing complex), and STAGA (SPT3-TAF9-GCN5L acetylase). PCAF (GCN5) and KAT2A (GCN5L) are two human homologs of the yeast Gcn5.[5] TAF8, TAF10, and SPT7L forms a small TAF complex called SMAT.[1] StructureThe N-terminal domain of TAF has a histone-like protein fold. It contains two short alpha helices and a long central alpha helix.[6] Human genes{{missing information|section|TAFs in non-TF2D complexes|date=April 2019}}
Assorted signaturesTAF domains are spread out across many digital signatures: |