1tba

Structural highlights

Function

[TAF1_DROME] TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Largest component and core scaffold of the complex. Contains N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. The C-terminal Ser/Thr kinase domain phosphorylates histone H2B at 'Ser-33', which may contribute to transcriptional activation during embryogenesis. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle. Negative regulator of the TATA box-binding activity of Tbp.^{[1] [2] [3] [4]} [TBP_YEAST] General transcription factor that functions at the core of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.^{[5] [6] [7]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Heat Shock Protein structures
• TATA-Binding Protein
• Transcription initiation factor

References

1. ↑ Kokubo T, Gong DW, Yamashita S, Horikoshi M, Roeder RG, Nakatani Y. Drosophila 230-kD TFIID subunit, a functional homolog of the human cell cycle gene product, negatively regulates DNA binding of the TATA box-binding subunit of TFIID. Genes Dev. 1993 Jun;7(6):1033-46. PMID:8504928
2. ↑ Dikstein R, Ruppert S, Tjian R. TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74. Cell. 1996 Mar 8;84(5):781-90. PMID:8625415
3. ↑ Maile T, Kwoczynski S, Katzenberger RJ, Wassarman DA, Sauer F. TAF1 activates transcription by phosphorylation of serine 33 in histone H2B. Science. 2004 May 14;304(5673):1010-4. PMID:15143281 doi:http://dx.doi.org/10.1126/science.1095001
4. ↑ Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M. Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP. Cell. 1998 Sep 4;94(5):573-83. PMID:9741622
5. ↑ Hampsey M. Molecular genetics of the RNA polymerase II general transcriptional machinery. Microbiol Mol Biol Rev. 1998 Jun;62(2):465-503. PMID:9618449
6. ↑ Sanders SL, Garbett KA, Weil PA. Molecular characterization of Saccharomyces cerevisiae TFIID. Mol Cell Biol. 2002 Aug;22(16):6000-13. PMID:12138208
7. ↑ Martinez E. Multi-protein complexes in eukaryotic gene transcription. Plant Mol Biol. 2002 Dec;50(6):925-47. PMID:12516863
8. ↑ Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M. Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP. Cell. 1998 Sep 4;94(5):573-83. PMID:9741622