Biology:TAF protein
| TAF | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 drosophila tbp associated factors dtafii42/dtafii62 heterotetramer | |||||||||
| Identifiers | |||||||||
| Symbol | TAF | ||||||||
| Pfam | PF02969 | ||||||||
| Pfam clan | CL0012 | ||||||||
| InterPro | IPR004823 | ||||||||
| SMART | TAFH | ||||||||
| SCOP2 | 1bh9 / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, TAF refers to a protein named the TATA-binding protein associated factor. TAF is part of the transcription initiation factor TFIID multimeric protein complex, or in simpler terms, the Pre-initiation complex (PIC). TAF forms part of Transcription factor II D (TFIID) and the TATA-binding protein (TBP). They mediate transcription of DNA to RNA by RNA polymerase II. This entry discusses the N-terminal domain in particular.
TFIID
TFIID 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).[1] TAF proteins adopt a histone-like fold.
TAF function
TAF is part of the TFIID complex, and interacts with the following:
- Specific transcriptional activators
- Basal transcription factors
- Other TAFIIs
- Specific DNA sequences, for example the downstream promoter element or gene-specific core promoter sequence
Due to such interactions, they therefore contribute transcription activation and to promoter selectivity.[1]
TAF structure
The N-terminal domain of TAF has a histone-like protein fold. It contains two short alpha helices and a long central alpha helix.[2]
Types of TAF
- TAF1 (TAFII250)
- TAF2 (CIF150)
- TAF3 (TAFII140)
- TAF4 (TAFII130/135)
- TAF4B (TAFII105)
- TAF5 (TAFII100)
- TAF6 (TAFII70/80)
- TAF7 (TAFII55)
- TAF8 (TAFII43)
- TAF9 (TAFII31/32)
- TAF9B (TAFII31L)
- TAF10 (TAFII30)
- TAF11 (TAFII28)
- TAF12 (TAFII20/15)
- TAF13 (TAFII18)
- TAF15 (TAFII68)
References
- ↑ 1.0 1.1 Furukawa T, Tanese N (2000). "Assembly of partial TFIID complexes in mammalian cells reveals distinct activities associated with individual TATA box-binding protein-associated factors.". J Biol Chem 275 (38): 29847–56. doi:10.1074/jbc.M002989200. PMID 10896937. https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=10896937.
- ↑ "Structural similarity between TAFs and the heterotetrameric core of the histone octamer.". Nature 380 (6572): 316–22. 1996. doi:10.1038/380316a0. PMID 8598927. https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=8598927.
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