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| | ==Crystal structure of the human TAF5-TAF6-TAF9 complex== | | ==Crystal structure of the human TAF5-TAF6-TAF9 complex== |
| - | <StructureSection load='6f3t' size='340' side='right' caption='[[6f3t]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='6f3t' size='340' side='right'caption='[[6f3t]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6f3t]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F3T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6f3t]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F3T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAF5, TAF2D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TAF6, TAF2E, TAFII70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TAF9, TAF2G, TAFII31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6f3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f3t OCA], [https://pdbe.org/6f3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f3t RCSB], [https://www.ebi.ac.uk/pdbsum/6f3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f3t ProSAT]</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=6f3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f3t OCA], [http://pdbe.org/6f3t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f3t RCSB], [http://www.ebi.ac.uk/pdbsum/6f3t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f3t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TAF5_HUMAN TAF5_HUMAN]] TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription. TAF5/TAFII100 interacts strongly with the histone H4-related TAF6/TAFII80 and the histone H3-related TAF9/TAFII31, as well as a stable complex comprised of both TAF5/TAFII80 and TAF6/TAFII31. Apparently weaker interactions of TAF5/TAFII100 with TBP, TAF1/TAFII250, TAF11/TAFII28, and TAF12/TAFII20, but not TAF7/TAFII55, also have been observed. [[http://www.uniprot.org/uniprot/TAF9_HUMAN TAF9_HUMAN]] Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription.<ref>PMID:15899866</ref> [[http://www.uniprot.org/uniprot/TAF6_HUMAN TAF6_HUMAN]] TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. | + | [https://www.uniprot.org/uniprot/TAF5_HUMAN TAF5_HUMAN] TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription. TAF5/TAFII100 interacts strongly with the histone H4-related TAF6/TAFII80 and the histone H3-related TAF9/TAFII31, as well as a stable complex comprised of both TAF5/TAFII80 and TAF6/TAFII31. Apparently weaker interactions of TAF5/TAFII100 with TBP, TAF1/TAFII250, TAF11/TAFII28, and TAF12/TAFII20, but not TAF7/TAFII55, also have been observed. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6f3t" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6f3t" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Berger, I]] | + | [[Category: Large Structures]] |
| - | [[Category: Haffke, M]] | + | [[Category: Berger I]] |
| - | [[Category: Complex]] | + | [[Category: Haffke M]] |
| - | [[Category: Taf]]
| + | |
| - | [[Category: Tbd-associated factor]]
| + | |
| - | [[Category: Tfiid]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
TAF5_HUMAN TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription. TAF5/TAFII100 interacts strongly with the histone H4-related TAF6/TAFII80 and the histone H3-related TAF9/TAFII31, as well as a stable complex comprised of both TAF5/TAFII80 and TAF6/TAFII31. Apparently weaker interactions of TAF5/TAFII100 with TBP, TAF1/TAFII250, TAF11/TAFII28, and TAF12/TAFII20, but not TAF7/TAFII55, also have been observed.
Publication Abstract from PubMed
TFIID is a cornerstone of eukaryotic gene regulation. Distinct TFIID complexes with unique subunit compositions exist and several TFIID subunits are shared with other complexes, thereby conveying precise cellular control of subunit allocation and functional assembly of this essential transcription factor. However, the molecular mechanisms that underlie the regulation of TFIID remain poorly understood. Here we use quantitative proteomics to examine TFIID submodules and assembly mechanisms in human cells. Structural and mutational analysis of the cytoplasmic TAF5-TAF6-TAF9 submodule identified novel interactions that are crucial for TFIID integrity and for allocation of TAF9 to TFIID or the Spt-Ada-Gcn5 acetyltransferase (SAGA) co-activator complex. We discover a key checkpoint function for the chaperonin CCT, which specifically associates with nascent TAF5 for subsequent handover to TAF6-TAF9 and ultimate holo-TFIID formation. Our findings illustrate at the molecular level how multisubunit complexes are generated within the cell via mechanisms that involve checkpoint decisions facilitated by a chaperone.
Chaperonin CCT checkpoint function in basal transcription factor TFIID assembly.,Antonova SV, Haffke M, Corradini E, Mikuciunas M, Low TY, Signor L, van Es RM, Gupta K, Scheer E, Vos HR, Tora L, Heck AJR, Timmers HTM, Berger I Nat Struct Mol Biol. 2018 Dec;25(12):1119-1127. doi: 10.1038/s41594-018-0156-z., Epub 2018 Dec 3. PMID:30510221[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Antonova SV, Haffke M, Corradini E, Mikuciunas M, Low TY, Signor L, van Es RM, Gupta K, Scheer E, Vos HR, Tora L, Heck AJR, Timmers HTM, Berger I. Chaperonin CCT checkpoint function in basal transcription factor TFIID assembly. Nat Struct Mol Biol. 2018 Dec;25(12):1119-1127. doi: 10.1038/s41594-018-0156-z., Epub 2018 Dec 3. PMID:30510221 doi:http://dx.doi.org/10.1038/s41594-018-0156-z
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