4oy2

From Proteopedia

(Difference between revisions)

Revision as of 22:42, 5 August 2016

Crystal structure of TAF1-TAF7, a TFIID subcomplex

Structural highlights

4oy2 is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
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] [TAF7_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. TAF7 is responsible for the recruitment of BDF1 to TATA element containing promoters.^[5] ^[6] ^[7] ^[8]

Publication Abstract from PubMed

Transcription factor II D (TFIID) is a multiprotein complex that nucleates formation of the basal transcription machinery. TATA binding protein-associated factors 1 and 7 (TAF1 and TAF7), two subunits of TFIID, are integral to the regulation of eukaryotic transcription initiation and play key roles in preinitiation complex (PIC) assembly. Current models suggest that TAF7 acts as a dissociable inhibitor of TAF1 histone acetyltransferase activity and that this event ensures appropriate assembly of the RNA polymerase II-mediated PIC before transcriptional initiation. Here, we report the 3D structure of a complex of yeast TAF1 with TAF7 at 2.9 A resolution. The structure displays novel architecture and is characterized by a large predominantly hydrophobic heterodimer interface and extensive cofolding of TAF subunits. There are no obvious similarities between TAF1 and known histone acetyltransferases. Instead, the surface of the TAF1-TAF7 complex contains two prominent conserved surface pockets, one of which binds selectively to an inhibitory trimethylated histone H3 mark on Lys27 in a manner that is also regulated by phosphorylation at the neighboring H3 serine. Our findings could point toward novel roles for the TAF1-TAF7 complex in regulation of PIC assembly via reading epigenetic histone marks.

Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D.,Bhattacharya S, Lou X, Hwang P, Rajashankar KR, Wang X, Gustafsson JA, Fletterick RJ, Jacobson RH, Webb P Proc Natl Acad Sci U S A. 2014 Jun 10. pii: 201408293. PMID:24927529^[9]

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
↑ 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
↑ Matangkasombut O, Buratowski RM, Swilling NW, Buratowski S. Bromodomain factor 1 corresponds to a missing piece of yeast TFIID. Genes Dev. 2000 Apr 15;14(8):951-62. PMID:10783167
↑ 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
↑ Bhattacharya S, Lou X, Hwang P, Rajashankar KR, Wang X, Gustafsson JA, Fletterick RJ, Jacobson RH, Webb P. Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D. Proc Natl Acad Sci U S A. 2014 Jun 10. pii: 201408293. PMID:24927529 doi:http://dx.doi.org/10.1073/pnas.1408293111

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4oy2"

@@ Line 1: / Line 1: @@
 ==Crystal structure of TAF1-TAF7, a TFIID subcomplex==
 <StructureSection load='4oy2' size='340' side='right' caption='[[4oy2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oy2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oy2 RCSB], [http://www.ebi.ac.uk/pdbsum/4oy2 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oy2 OCA], [http://pdbe.org/4oy2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oy2 RCSB], [http://www.ebi.ac.uk/pdbsum/4oy2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oy2 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4oy2" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Transcription initiation factor|Transcription initiation factor]]
 == References ==
 <references/>

4oy2

From Proteopedia

Revision as of 22:42, 5 August 2016

Crystal structure of TAF1-TAF7, a TFIID subcomplex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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