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==SAGA Tra1 module==
==SAGA Tra1 module==
<StructureSection load='6t9j' size='340' side='right'caption='[[6t9j]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<SX load='6t9j' size='340' side='right' viewer='molstar' caption='[[6t9j]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6t9j]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T9J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6T9J FirstGlance]. <br>
<table><tr><td colspan='2'>[[6t9j]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T9J FirstGlance]. <br>
</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=6t9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t9j OCA], [http://pdbe.org/6t9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t9j RCSB], [http://www.ebi.ac.uk/pdbsum/6t9j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t9j ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</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=6t9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t9j OCA], [https://pdbe.org/6t9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t9j RCSB], [https://www.ebi.ac.uk/pdbsum/6t9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t9j ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SPT20_YEAST SPT20_YEAST]] Transcription regulator. May recruit TATA binding protein (TBP) and possibly other basal factors to bind to the TATA box. Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.<ref>PMID:10026213</ref>  [[http://www.uniprot.org/uniprot/TRA1_YEAST TRA1_YEAST]] Essential component of histone acetyltransferase (HAT) complexes, which serves as a target for activators during recruitment of HAT complexes. Essential for vegetative growth. Functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.<ref>PMID:10026213</ref> <ref>PMID:11423663</ref> [[http://www.uniprot.org/uniprot/TAF12_YEAST TAF12_YEAST]] Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. 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. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.<ref>PMID:10026213</ref> <ref>PMID:10788514</ref> <ref>PMID:11238921</ref> <ref>PMID:11295558</ref> <ref>PMID:11473260</ref> <ref>PMID:12052880</ref> <ref>PMID:12138208</ref> <ref>PMID:12516863</ref> <ref>PMID:9674426</ref> <ref>PMID:9695952</ref> 
[https://www.uniprot.org/uniprot/TRA1_YEAST TRA1_YEAST] Essential component of histone acetyltransferase (HAT) complexes, which serves as a target for activators during recruitment of HAT complexes. Essential for vegetative growth. Functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.<ref>PMID:10026213</ref> <ref>PMID:11423663</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Gene transcription by RNA polymerase II is regulated by activator proteins that recruit the coactivator complexes SAGA (Spt-Ada-Gcn5-acetyltransferase)(1,2) and transcription factor IID (TFIID)(2-4). SAGA is required for all regulated transcription(5) and is conserved among eukaryotes(6). SAGA contains four modules(7-9): the activator-binding Tra1 module, the core module, the histone acetyltransferase (HAT) module and the histone deubiquitination (DUB) module. Previous studies provided partial structures(10-14), but the structure of the central core module is unknown. Here we present the cryo-electron microscopy structure of SAGA from the yeast Saccharomyces cerevisiae and resolve the core module at 3.3 A resolution. The core module consists of subunits Taf5, Sgf73 and Spt20, and a histone octamer-like fold. The octamer-like fold comprises the heterodimers Taf6-Taf9, Taf10-Spt7 and Taf12-Ada1, and two histone-fold domains in Spt3. Spt3 and the adjacent subunit Spt8 interact with the TATA box-binding protein (TBP)(2,7,15-17). The octamer-like fold and its TBP-interacting region are similar in TFIID, whereas Taf5 and the Taf6 HEAT domain adopt distinct conformations. Taf12 and Spt20 form flexible connections to the Tra1 module, whereas Sgf73 tethers the DUB module. Binding of a nucleosome to SAGA displaces the HAT and DUB modules from the core-module surface, allowing the DUB module to bind one face of an ubiquitinated nucleosome.
 
Structure of the transcription coactivator SAGA.,Wang H, Dienemann C, Stutzer A, Urlaub H, Cheung ACM, Cramer P Nature. 2020 Jan;577(7792):717-720. doi: 10.1038/s41586-020-1933-5. Epub 2020 Jan, 22. PMID:31969703<ref>PMID:31969703</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6t9j" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cheung, A]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Cramer, P]]
[[Category: Cheung A]]
[[Category: Wang, H]]
[[Category: Cramer P]]
[[Category: Coactivator]]
[[Category: Wang H]]
[[Category: Gene regulation]]
[[Category: Histone acetyltransferase]]
[[Category: Histone deubiquitinase]]
[[Category: Transcription]]

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