| Structural highlights
4b0a is a 1 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Related: | 1ngm, 1nh2, 1rm1, 1tba, 1tbp, 1ytb, 1ytf |
| Activity: | Histone acetyltransferase, with EC number 2.3.1.48 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[TAF1_YEAST] Functions as a component 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 pre-initiation 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.[1] [2] [3] [4]
Publication Abstract from PubMed
The general transcription factor TFIID provides a regulatory platform for transcription initiation. Here we present the crystal structure (1.97 A) and NMR analysis of yeast TAF1 N-terminal domains TAND1 and TAND2 bound to yeast TBP, together with mutational data. We find that yeast TAF1-TAND1, which in itself acts as a transcriptional activator, binds TBP's concave DNA-binding surface by presenting similar anchor residues to TBP as does Mot1 but from a distinct structural scaffold. Furthermore, we show how TAF1-TAND2 uses an aromatic and acidic anchoring pattern to bind a conserved TBP surface groove traversing the basic helix region, and we find highly similar TBP-binding motifs also presented by the structurally distinct TFIIA, Mot1 and Brf1 proteins. Our identification of these anchoring patterns, which can be easily disrupted or enhanced, provides insight into the competitive multiprotein TBP interplay critical to transcriptional regulation.
High-resolution structure of TBP with TAF1 reveals anchoring patterns in transcriptional regulation.,Anandapadamanaban M, Andresen C, Helander S, Ohyama Y, Siponen MI, Lundstrom P, Kokubo T, Ikura M, Moche M, Sunnerhagen M Nat Struct Mol Biol. 2013 Jul 14. doi: 10.1038/nsmb.2611. PMID:23851461[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mizzen CA, Yang XJ, Kokubo T, Brownell JE, Bannister AJ, Owen-Hughes T, Workman J, Wang L, Berger SL, Kouzarides T, Nakatani Y, Allis CD. The TAF(II)250 subunit of TFIID has histone acetyltransferase activity. Cell. 1996 Dec 27;87(7):1261-70. PMID:8980232
- ↑ Sanders SL, Weil PA. Identification of two novel TAF subunits of the yeast Saccharomyces cerevisiae TFIID complex. J Biol Chem. 2000 May 5;275(18):13895-900. PMID:10788514
- ↑ Sanders SL, Garbett KA, Weil PA. Molecular characterization of Saccharomyces cerevisiae TFIID. Mol Cell Biol. 2002 Aug;22(16):6000-13. PMID:12138208
- ↑ Martinez E. Multi-protein complexes in eukaryotic gene transcription. Plant Mol Biol. 2002 Dec;50(6):925-47. PMID:12516863
- ↑ Anandapadamanaban M, Andresen C, Helander S, Ohyama Y, Siponen MI, Lundstrom P, Kokubo T, Ikura M, Moche M, Sunnerhagen M. High-resolution structure of TBP with TAF1 reveals anchoring patterns in transcriptional regulation. Nat Struct Mol Biol. 2013 Jul 14. doi: 10.1038/nsmb.2611. PMID:23851461 doi:10.1038/nsmb.2611
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