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Open data
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Basic information
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| Title | Cryo-EM structure of the human SAGA co-activator complex | |||||||||
Map data | Composite map of human SAGA | |||||||||
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Keywords | Transcription co-activator / Lysine acetyltransferase / complex / TRANSCRIPTION | |||||||||
| Function / homology | Function and homology informationSAGA-type complex / regulation of somatic stem cell population maintenance / SAGA complex assembly / lateral mesodermal cell differentiation / allantois development / transcription factor TFTC complex / SLIK (SAGA-like) complex / negative regulation of microtubule depolymerization / somitogenesis / embryonic placenta development ...SAGA-type complex / regulation of somatic stem cell population maintenance / SAGA complex assembly / lateral mesodermal cell differentiation / allantois development / transcription factor TFTC complex / SLIK (SAGA-like) complex / negative regulation of microtubule depolymerization / somitogenesis / embryonic placenta development / nucleus organization / Swr1 complex / U12-type spliceosomal complex / SAGA complex / maintenance of protein location in nucleus / RNA splicing, via transesterification reactions / splicing factor binding / U2-type precatalytic spliceosome / RNA polymerase binding / U2-type prespliceosome assembly / U2-type spliceosomal complex / regulation of double-strand break repair / U2 snRNP / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / transcription preinitiation complex / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / precatalytic spliceosome / transcription factor TFIID complex / RNA polymerase II general transcription initiation factor activity / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / histone deacetylase complex / regulation of RNA splicing / mRNA Splicing - Minor Pathway / NuA4 histone acetyltransferase complex / DNA repair-dependent chromatin remodeling / limb development / gastrulation / positive regulation of transcription initiation by RNA polymerase II / U2 snRNA binding / RNA polymerase II preinitiation complex assembly / positive regulation of double-strand break repair via homologous recombination / spliceosomal snRNP assembly / visual perception / catalytic step 2 spliceosome / RNA Polymerase II Pre-transcription Events / mRNA Splicing - Major Pathway / RNA splicing / regulation of DNA repair / TBP-class protein binding / nuclear estrogen receptor binding / negative regulation of protein catabolic process / promoter-specific chromatin binding / DNA-templated transcription initiation / mRNA splicing, via spliceosome / transcription initiation at RNA polymerase II promoter / microtubule cytoskeleton organization / mRNA transcription by RNA polymerase II / Formation of the beta-catenin:TCF transactivating complex / transcription by RNA polymerase II / autophagy / transcription coregulator activity / mRNA Polyadenylation / nuclear matrix / microtubule cytoskeleton / transcription corepressor activity / positive regulation of cell growth / HATs acetylate histones / Dengue Virus-Host Interactions / DNA-binding transcription factor binding / Regulation of TP53 Activity through Phosphorylation / regulation of apoptotic process / regulation of cell cycle / transcription coactivator activity / nuclear speck / protein stabilization / Ub-specific processing proteases / chromatin remodeling / protein heterodimerization activity / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / nucleolus / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / protein-containing complex binding / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / enzyme binding / positive regulation of transcription by RNA polymerase II / DNA binding / DNA-templated transcription / RNA binding / extracellular exosome / nucleoplasm / identical protein binding Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.41 Å | |||||||||
Authors | Damilot M / Ben-Shem A / Papai G | |||||||||
| Funding support | France, 2 items
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Citation | Journal: Sci Adv / Year: 2026Title: Insights into the structure and evolution of the human SAGA complex by affinity-ligand purification. Authors: Mylène Damilot / Thomas Schoeps / Laszlo Tora / Patrick Schultz / Luc Lebeau / Gabor Papai / Adam Ben-Shem / ![]() Abstract: Human SAGA is a 20-subunit transcriptional coactivator. Compared with yeast, metazoan SAGA uniquely incorporates a 150-kDa splicing-factor module (SPL), also present in U2 small nuclear ...Human SAGA is a 20-subunit transcriptional coactivator. Compared with yeast, metazoan SAGA uniquely incorporates a 150-kDa splicing-factor module (SPL), also present in U2 small nuclear ribonucleoprotein (U2snRNP). Metazoan gene duplication further specialized shared TFIID/SAGA subunits into SAGA-specific paralogs (TAF5L and TAF6L), but the functional consequences of this divergence are unknown. We report the structure of endogenous human SAGA purified via an affinity ligand from cells that were not disturbed by any genomic engineering tools. Our work reveals the high-resolution structure of SPL and the TAF6L HEAT repeat domain that provides the SPL with a docking surface. We elucidate how SPL and the HEAT repeats are incorporated into SAGA. We identify major structural differences between TAF6L/TAF5L and their canonical paralogs that enable SPL accommodation. SPL engages SAGA through a substantially smaller interface than in U2snRNP, despite sharing a deeply inserted helical motif. The seemingly weaker interaction of SPL with SAGA raises the possibility that SAGA relays this module to the splicing machinery. | |||||||||
| History |
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_53937.map.gz | 8.4 MB | EMDB map data format | |
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| Header (meta data) | emd-53937-v30.xml emd-53937.xml | 34.1 KB 34.1 KB | Display Display | EMDB header |
| Images | emd_53937.png | 69.7 KB | ||
| Filedesc metadata | emd-53937.cif.gz | 12.3 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-53937 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-53937 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9rdkMC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_53937.map.gz / Format: CCP4 / Size: 259.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Composite map of human SAGA | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : SAGA
+Supramolecule #1: SAGA
+Macromolecule #1: Transcription initiation factor TFIID subunit 9B
+Macromolecule #2: Ataxin-7
+Macromolecule #3: TAF5-like RNA polymerase II p300/CBP-associated factor-associated...
+Macromolecule #4: Splicing factor 3B subunit 3
+Macromolecule #5: Transformation/transcription domain-associated protein
+Macromolecule #6: STAGA complex 65 subunit gamma
+Macromolecule #7: Transcription initiation factor TFIID subunit 12
+Macromolecule #8: Transcription initiation factor TFIID subunit 10
+Macromolecule #9: Transcription initiation protein SPT3 homolog
+Macromolecule #10: Transcriptional adapter 1
+Macromolecule #11: TAF6-like RNA polymerase II p300/CBP-associated factor-associated...
+Macromolecule #12: Transcription factor SPT20 homolog
+Macromolecule #13: Splicing factor 3B subunit 5
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.15 mg/mL |
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| Buffer | pH: 8 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.2 µm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
France, 2 items
Citation












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Processing
FIELD EMISSION GUN
