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- PDB-6yov: OCT4-SOX2-bound nucleosome - SHL+6 -

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Basic information

Entry
Database: PDB / ID: 6yov
TitleOCT4-SOX2-bound nucleosome - SHL+6
Components
  • (Histone H3.1Histone H3) x 2
  • (Histone H4) x 2
  • DNA (142-MER)
  • Green fluorescent protein,POU domain, class 5, transcription factor 1
  • Histone H2A type 1-B/E
  • Histone H2B type 1-J
  • Transcription factor SOX-2
KeywordsTRANSCRIPTION / nucleosome / OCT4 / SOX2 / transcription factor
Function / homology
Function and homology information


cell fate commitment involved in formation of primary germ layer / regulation of heart induction by regulation of canonical Wnt signaling pathway / regulation of DNA methylation-dependent heterochromatin assembly / glial cell fate commitment / POU5F1 (OCT4), SOX2, NANOG repress genes related to differentiation / cardiac cell fate determination / regulation of asymmetric cell division / endodermal cell fate specification / BMP signaling pathway involved in heart induction / adenohypophysis development ...cell fate commitment involved in formation of primary germ layer / regulation of heart induction by regulation of canonical Wnt signaling pathway / regulation of DNA methylation-dependent heterochromatin assembly / glial cell fate commitment / POU5F1 (OCT4), SOX2, NANOG repress genes related to differentiation / cardiac cell fate determination / regulation of asymmetric cell division / endodermal cell fate specification / BMP signaling pathway involved in heart induction / adenohypophysis development / POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation / Transcriptional regulation of pluripotent stem cells / Transcriptional Regulation by MECP2 / regulation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of cell-cell adhesion / pituitary gland development / neuronal stem cell population maintenance / eye development / response to growth factor / tissue regeneration / blastocyst development / miRNA binding / negative regulation of gene silencing by miRNA / somatic stem cell population maintenance / positive regulation of SMAD protein signal transduction / negative regulation of megakaryocyte differentiation / Packaging Of Telomere Ends / inner ear development / depurination / negative regulation of pri-miRNA transcription by RNA polymerase II / positive regulation of histone exchange / CENP-A containing nucleosome assembly / negative regulation of tumor necrosis factor-mediated signaling pathway / Chromatin modifying enzymes / Deposition of new CENPA-containing nucleosomes at the centromere / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / negative regulation of neuron differentiation / negative regulation of DNA recombination at telomere / DNA replication-independent nucleosome assembly / anatomical structure morphogenesis / telomere capping / Inhibition of DNA recombination at telomere / Cleavage of the damaged pyrimidine / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / interleukin-7-mediated signaling pathway / Meiotic synapsis / cell fate commitment / chromatin silencing / RNA Polymerase I Promoter Opening / telomere organization / SUMOylation of chromatin organization proteins / Interleukin-7 signaling / DNA replication-dependent nucleosome assembly / forebrain development / DNA methylation / HCMV Late Events / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / rDNA heterochromatin assembly / SIRT1 negatively regulates rRNA expression / innate immune response in mucosa / Condensation of Prophase Chromosomes / PRC2 methylates histones and DNA / negative regulation of gene expression, epigenetic / regulation of gene silencing / RNA Polymerase I Promoter Escape / mitotic chromosome condensation / bioluminescence / positive regulation of cell differentiation / regulation of gene silencing by miRNA / osteoblast differentiation / HDACs deacetylate histones / Nonhomologous End-Joining (NHEJ) / generation of precursor metabolites and energy / nuclear chromosome / NoRC negatively regulates rRNA expression / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / DNA-templated transcription, initiation / B-WICH complex positively regulates rRNA expression / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Deactivation of the beta-catenin transactivating complex / regulation of megakaryocyte differentiation / Metalloprotease DUBs / nucleosome assembly / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / G2/M DNA damage checkpoint / DNA Damage/Telomere Stress Induced Senescence / lipopolysaccharide binding / RMTs methylate histone arginines / HCMV Early Events / DNA-binding transcription repressor activity, RNA polymerase II-specific / regulation of androgen receptor signaling pathway / Pre-NOTCH Transcription and Translation / PKMTs methylate histone lysines / nucleosome / HDMs demethylate histones / Meiotic recombination / Activation of anterior HOX genes in hindbrain development during early embryogenesis / UCH proteinases
Similarity search - Function
POU domain-containing protein, class 5 / Transcription factor SOX-2 / Transcription factor SOX / SOX transcription factor / POU-specific domain / POU-specific (POUs) domain profile. / POU-specific (POUs) domain signature 2. / POU-specific (POUs) domain signature 1. / Pou domain - N-terminal to homeobox domain / POU domain ...POU domain-containing protein, class 5 / Transcription factor SOX-2 / Transcription factor SOX / SOX transcription factor / POU-specific domain / POU-specific (POUs) domain profile. / POU-specific (POUs) domain signature 2. / POU-specific (POUs) domain signature 1. / Pou domain - N-terminal to homeobox domain / POU domain / Found in Pit-Oct-Unc transcription factors / High mobility group box domain / DNA Binding (I), subunit A / Homeobox, conserved site / 'Homeobox' domain signature. / Homeodomain / 'Homeobox' domain profile. / Homeodomain / Homeobox domain / lambda repressor-like DNA-binding domains / HMG (high mobility group) box / HMG boxes A and B DNA-binding domains profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily / Histone, subunit A / Histone, subunit A / 434 Repressor (Amino-terminal Domain) / Lambda repressor-like, DNA-binding domain superfamily / Histone H2B / Histone H2B signature. / Histone H2B / Histone H2A conserved site / Histone H2A signature. / C-terminus of histone H2A / Histone H2A, C-terminal domain / Histone H2A / Histone 2A / Green fluorescent protein, GFP / Histone H4 / Histone H4, conserved site / Histone H4 signature. / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF) / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Core histone H2A/H2B/H3/H4 / Histone H2A/H2B/H3 / Histone-fold / Homeobox-like domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Histone H3.1 / Histone H4 / Transcription factor SOX-2 / Green fluorescent protein / PENTANEDIAL / Histone H2B type 1-J / Histone H2A type 1-B/E / DNA (> 100) / DNA (> 10) / DNA / POU domain, class 5, transcription factor 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Aequorea victoria (jellyfish)
synthetic construct (others)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.42 Å
AuthorsMichael, A.K. / Kempf, G. / Cavadini, S. / Bunker, R.D. / Thoma, N.H.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Swiss National Science FoundationCRSII3_160734/1 Switzerland
CitationJournal: Science / Year: 2020
Title: Mechanisms of OCT4-SOX2 motif readout on nucleosomes.
Authors: Alicia K Michael / Ralph S Grand / Luke Isbel / Simone Cavadini / Zuzanna Kozicka / Georg Kempf / Richard D Bunker / Andreas D Schenk / Alexandra Graff-Meyer / Ganesh R Pathare / Joscha ...Authors: Alicia K Michael / Ralph S Grand / Luke Isbel / Simone Cavadini / Zuzanna Kozicka / Georg Kempf / Richard D Bunker / Andreas D Schenk / Alexandra Graff-Meyer / Ganesh R Pathare / Joscha Weiss / Syota Matsumoto / Lukas Burger / Dirk Schübeler / Nicolas H Thomä /
Abstract: Transcription factors (TFs) regulate gene expression through chromatin where nucleosomes restrict DNA access. To study how TFs bind nucleosome-occupied motifs, we focused on the reprogramming factors ...Transcription factors (TFs) regulate gene expression through chromatin where nucleosomes restrict DNA access. To study how TFs bind nucleosome-occupied motifs, we focused on the reprogramming factors OCT4 and SOX2 in mouse embryonic stem cells. We determined TF engagement throughout a nucleosome at base-pair resolution in vitro, enabling structure determination by cryo-electron microscopy at two preferred positions. Depending on motif location, OCT4 and SOX2 differentially distort nucleosomal DNA. At one position, OCT4-SOX2 removes DNA from histone H2A and histone H3; however, at an inverted motif, the TFs only induce local DNA distortions. OCT4 uses one of its two DNA-binding domains to engage DNA in both structures, reading out a partial motif. These findings explain site-specific nucleosome engagement by the pluripotency factors OCT4 and SOX2, and they reveal how TFs distort nucleosomes to access chromatinized motifs.
History
DepositionApr 15, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 6, 2020Provider: repository / Type: Initial release
Revision 1.1May 13, 2020Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation_author.identifier_ORCID
Revision 1.2Jul 8, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last

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Structure visualization

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Assembly

Deposited unit
A: Histone H3.1
B: Histone H4
C: Histone H2A type 1-B/E
D: Histone H2B type 1-J
E: Histone H3.1
F: Histone H4
G: Histone H2A type 1-B/E
H: Histone H2B type 1-J
I: DNA (142-MER)
J: DNA (142-MER)
K: Green fluorescent protein,POU domain, class 5, transcription factor 1
L: Transcription factor SOX-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)379,45620
Polymers378,65512
Non-polymers8018
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: native gel electrophoresis
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 8 types, 10 molecules ABCGDHEFKL

#1: Protein Histone H3.1 / Histone H3 / Histone H3/a / Histone H3/b / Histone H3/c / Histone H3/d / Histone H3/f / Histone H3/h / Histone ...Histone H3/a / Histone H3/b / Histone H3/c / Histone H3/d / Histone H3/f / Histone H3/h / Histone H3/i / Histone H3/j / Histone H3/k / Histone H3/l


Mass: 15719.445 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: HIST1H3A, H3FA, HIST1H3B, H3FL, HIST1H3C, H3FC, HIST1H3D, H3FB, HIST1H3E, H3FD, HIST1H3F, H3FI, HIST1H3G, H3FH, HIST1H3H, H3FK, HIST1H3I, H3FF, HIST1H3J, H3FJ
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P68431
#2: Protein Histone H4 /


Mass: 11547.523 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: H4C1, H4/A, H4FA, HIST1H4A, H4C2, H4/I, H4FI, HIST1H4B, H4C3, H4/G, H4FG, HIST1H4C, H4C4, H4/B, H4FB, HIST1H4D, H4C5, H4/J, H4FJ, HIST1H4E, H4C6, H4/C, H4FC, HIST1H4F, H4C8, H4/H, H4FH, ...Gene: H4C1, H4/A, H4FA, HIST1H4A, H4C2, H4/I, H4FI, HIST1H4B, H4C3, H4/G, H4FG, HIST1H4C, H4C4, H4/B, H4FB, HIST1H4D, H4C5, H4/J, H4FJ, HIST1H4E, H4C6, H4/C, H4FC, HIST1H4F, H4C8, H4/H, H4FH, HIST1H4H, H4C9, H4/M, H4FM, HIST1H4I, H4C11, H4/E, H4FE, HIST1H4J, H4C12, H4/D, H4FD, HIST1H4K, H4C13, H4/K, H4FK, HIST1H4L, H4C14, H4/N, H4F2, H4FN, HIST2H4, HIST2H4A, H4C15, H4/O, H4FO, HIST2H4B, H4-16, HIST4H4
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P62805
#3: Protein Histone H2A type 1-B/E / Histone H2A.2 / Histone H2A/a / Histone H2A/m


Mass: 14447.825 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HIST1H2AB, H2AFM, HIST1H2AE, H2AFA
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P04908
#4: Protein Histone H2B type 1-J / Histone H2B.1 / Histone H2B.r / H2B/r


Mass: 14088.336 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HIST1H2BJ, H2BFR
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P06899
#5: Protein Histone H3.1 / Histone H3 / Histone H3/a / Histone H3/b / Histone H3/c / Histone H3/d / Histone H3/f / Histone H3/h / Histone ...Histone H3/a / Histone H3/b / Histone H3/c / Histone H3/d / Histone H3/f / Histone H3/h / Histone H3/i / Histone H3/j / Histone H3/k / Histone H3/l


Mass: 15491.173 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: H3C1, H3FA, HIST1H3A, H3C2, H3FL, HIST1H3B, H3C3, H3FC HIST1H3C, H3C4, H3FB, HIST1H3D, H3C6, H3FD, HIST1H3E, H3C7, H3FI, HIST1H3F, H3C8, H3FH, HIST1H3G, H3C10, H3FK, HIST1H3H, H3C11, H3FF, ...Gene: H3C1, H3FA, HIST1H3A, H3C2, H3FL, HIST1H3B, H3C3, H3FC HIST1H3C, H3C4, H3FB, HIST1H3D, H3C6, H3FD, HIST1H3E, H3C7, H3FI, HIST1H3F, H3C8, H3FH, HIST1H3G, H3C10, H3FK, HIST1H3H, H3C11, H3FF, HIST1H3I, H3C12, H3FJ, HIST1H3J
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P68431
#6: Protein Histone H4 /


Mass: 11676.703 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, ...Gene: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P62805
#8: Protein Green fluorescent protein,POU domain, class 5, transcription factor 1 / Octamer-binding protein 3 / Oct-3 / Octamer-binding protein 4 / Oct-4 / Octamer-binding ...Octamer-binding protein 3 / Oct-3 / Octamer-binding protein 4 / Oct-4 / Octamer-binding transcription factor 3 / OTF-3


Mass: 69137.789 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aequorea victoria (jellyfish), (gene. exp.) Homo sapiens (human)
Gene: GFP, POU5F1, OCT3, OCT4, OTF3 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P42212, UniProt: Q01860
#9: Protein Transcription factor SOX-2


Mass: 12718.679 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SOX2 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P48431

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DNA chain / Non-polymers , 2 types, 10 molecules IJ

#10: Chemical
ChemComp-PTD / PENTANEDIAL / Glutaraldehyde


Mass: 100.116 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C5H8O2 / Comment: medication*YM
#7: DNA chain DNA (142-MER)


Mass: 92645.859 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Details

Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

Component
IDNameTypeEntity IDParent-IDSource
1Ternary complex of OCT4-SOX2 and SHL+6 nucleosomeCOMPLEX#1-#90MULTIPLE SOURCES
2HistonesHistoneCOMPLEX#1-#61RECOMBINANT
3DNACOMPLEX#71RECOMBINANT
4Green fluorescent protein,POU domain, class 5, transcription factor 1COMPLEX#81RECOMBINANT
5SOX2COMPLEX#91RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
22Homo sapiens (human)9606
33synthetic construct (others)32630
65Homo sapiens (human)9606
74Homo sapiens (human)9606
84Aequorea victoria (jellyfish)6100
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-ID
22Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)866768
33synthetic construct (others)32630
44Trichoplusia ni (cabbage looper)7111
65Trichoplusia ni (cabbage looper)7111
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / C2 aperture diameter: 50 µm
Image recordingElectron dose: 45 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 QUANTUM (4k x 4k)

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Processing

EM software
IDNameVersionCategory
4gCTFCTF correction
13cryoSPARCv23D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.42 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 71284 / Symmetry type: POINT

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