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Open data
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Basic information
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Title | CX3CR1 nucleosome and wild type PU.1 complex | |||||||||
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Function / homology | ![]() positive regulation of myeloid dendritic cell chemotaxis / anatomical structure regression / follicular B cell differentiation / positive regulation of antifungal innate immune response / regulation of myeloid progenitor cell differentiation / pro-T cell differentiation / negative regulation of neutrophil degranulation / germinal center B cell differentiation / myeloid leukocyte differentiation / positive regulation of microglial cell mediated cytotoxicity ...positive regulation of myeloid dendritic cell chemotaxis / anatomical structure regression / follicular B cell differentiation / positive regulation of antifungal innate immune response / regulation of myeloid progenitor cell differentiation / pro-T cell differentiation / negative regulation of neutrophil degranulation / germinal center B cell differentiation / myeloid leukocyte differentiation / positive regulation of microglial cell mediated cytotoxicity / granulocyte differentiation / lymphocyte differentiation / apoptotic process involved in blood vessel morphogenesis / endothelial to hematopoietic transition / negative regulation of adipose tissue development / pericyte cell differentiation / immature B cell differentiation / negative regulation of MHC class II biosynthetic process / lymphoid progenitor cell differentiation / myeloid dendritic cell differentiation / vasculature development / regulation of DNA-binding transcription factor activity / oncogene-induced cell senescence / negative regulation of protein localization to chromatin / positive regulation of p38MAPK cascade / positive regulation of B cell differentiation / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Lian T / Guan R / Bai Y | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural mechanism of synergistic targeting of the CX3CR1 nucleosome by PU.1 and C/EBPα. Authors: Tengfei Lian / Ruifang Guan / Bing-Rui Zhou / Yawen Bai / ![]() Abstract: Pioneer transcription factors are vital for cell fate changes. PU.1 and C/EBPα work together to regulate hematopoietic stem cell differentiation. However, how they recognize in vivo nucleosomal DNA ...Pioneer transcription factors are vital for cell fate changes. PU.1 and C/EBPα work together to regulate hematopoietic stem cell differentiation. However, how they recognize in vivo nucleosomal DNA targets remains elusive. Here we report the structures of the nucleosome containing the mouse genomic CX3CR1 enhancer DNA and its complexes with PU.1 alone and with both PU.1 and the C/EBPα DNA binding domain. Our structures reveal that PU.1 binds the DNA motif at the exit linker, shifting 17 bp of DNA into the core region through interactions with H2A, unwrapping ~20 bp of nucleosomal DNA. C/EBPα binding, aided by PU.1's repositioning, unwraps ~25 bp of entry DNA. The PU.1 Q218H mutation, linked to acute myeloid leukemia, disrupts PU.1-H2A interactions. PU.1 and C/EBPα jointly displace linker histone H1 and open the H1-condensed nucleosome array. Our study unveils how two pioneer factors can work cooperatively to open closed chromatin by altering DNA positioning in the nucleosome. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 43.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 21.5 KB 21.5 KB | Display Display | ![]() |
Images | ![]() | 40.8 KB | ||
Filedesc metadata | ![]() | 6.7 KB | ||
Others | ![]() ![]() | 41.1 MB 41.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8evhMC ![]() 8eviC ![]() 8evjC ![]() 8sypC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.056 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_28629_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_28629_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : nucleosome PU.1 complex
Entire | Name: nucleosome PU.1 complex |
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Components |
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-Supramolecule #1: nucleosome PU.1 complex
Supramolecule | Name: nucleosome PU.1 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Histone H3.1
Macromolecule | Name: Histone H3.1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 15.437167 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEACEA YLVGLFEDTN LCAIHAKRVT IMPKDIQLAR RIRGERA UniProtKB: ![]() |
-Macromolecule #2: Histone H4
Macromolecule | Name: Histone H4 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 11.394426 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG UniProtKB: ![]() |
-Macromolecule #3: Histone H2A type 2-C
Macromolecule | Name: Histone H2A type 2-C / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 14.017428 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIR NDEELNKLLG KVTIAQGGVL PNIQAVLLPK KTESHKAKSK UniProtKB: Histone H2A type 2-C |
-Macromolecule #4: Histone H2B type 2-E
Macromolecule | Name: Histone H2B type 2-E / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 13.951239 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSSK UniProtKB: Histone H2B type 2-E |
-Macromolecule #7: Single-chain variable fragment
Macromolecule | Name: Single-chain variable fragment / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 29.030146 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MKSSHHHHHH ENLYFQSNAM EVQLQQSGPE LVEPGTSVKM PCKASGYTFT SYTIQWVKQT PRQGLEWIGY IYPYNAGTKY NEKFKGKAT LTSDKSSSTV YMELSSLTSE DSAVYYCARK SSRLRSTLDY WGQGTSVTVS SGGGGSGGGG SGGGGSMDIK M TQSPSSMH ...String: MKSSHHHHHH ENLYFQSNAM EVQLQQSGPE LVEPGTSVKM PCKASGYTFT SYTIQWVKQT PRQGLEWIGY IYPYNAGTKY NEKFKGKAT LTSDKSSSTV YMELSSLTSE DSAVYYCARK SSRLRSTLDY WGQGTSVTVS SGGGGSGGGG SGGGGSMDIK M TQSPSSMH ASLGERVTIT CKASQDIRSY LSWYQQKPWK SPKTLIYYAT SLADGVPSRF SGSGSGQDFS LTINNLESDD TA TYYCLQH GESPYTFGSG TKLEIKRA |
-Macromolecule #8: Transcription factor PU.1
Macromolecule | Name: Transcription factor PU.1 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 32.81975 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MGSSHHHHHH SSGMLQACKM EGFSLTAPPS DDLVTYDSEL YQRPMHDYYS FVGSDGESHS DHYWDFSAHH VHNNEFENFP ENHFTELQS VQPPQLQQLY RHMELEQMHV LDTPMVPPHT GLSHQVSYMP RMCFPYQTLS PAHQQSSDEE EGERQSPPLE V SDGEADGL ...String: MGSSHHHHHH SSGMLQACKM EGFSLTAPPS DDLVTYDSEL YQRPMHDYYS FVGSDGESHS DHYWDFSAHH VHNNEFENFP ENHFTELQS VQPPQLQQLY RHMELEQMHV LDTPMVPPHT GLSHQVSYMP RMCFPYQTLS PAHQQSSDEE EGERQSPPLE V SDGEADGL EPGPGLLHGE TGSKKKIRLY QFLLDLLRSG DMKDSIWWVD KDKGTFQFSS KHKEALAHRW GIQKGNRKKM TY QKMARAL RNYGKTGEVK KVKKKLTYQF SGEVLGRGGL AERRLPPH UniProtKB: Transcription factor PU.1 |
-Macromolecule #5: DNA (162-MER)
Macromolecule | Name: DNA (162-MER) / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 50.043855 KDa |
Sequence | String: (DT)(DA)(DG)(DG)(DT)(DG)(DC)(DA)(DG)(DG) (DG)(DC)(DC)(DT)(DC)(DT)(DC)(DG)(DG)(DC) (DT)(DG)(DC)(DT)(DG)(DA)(DT)(DC)(DT) (DT)(DC)(DA)(DG)(DC)(DT)(DG)(DG)(DT)(DT) (DG) (DC)(DT)(DG)(DA)(DG)(DA) ...String: (DT)(DA)(DG)(DG)(DT)(DG)(DC)(DA)(DG)(DG) (DG)(DC)(DC)(DT)(DC)(DT)(DC)(DG)(DG)(DC) (DT)(DG)(DC)(DT)(DG)(DA)(DT)(DC)(DT) (DT)(DC)(DA)(DG)(DC)(DT)(DG)(DG)(DT)(DT) (DG) (DC)(DT)(DG)(DA)(DG)(DA)(DG)(DT) (DT)(DG)(DC)(DA)(DG)(DC)(DA)(DT)(DT)(DG) (DC)(DT) (DG)(DA)(DG)(DT)(DC)(DT)(DT) (DA)(DG)(DC)(DA)(DA)(DT)(DG)(DG)(DA)(DT) (DA)(DC)(DT) (DT)(DC)(DC)(DC)(DG)(DA) (DT)(DT)(DC)(DC)(DC)(DC)(DT)(DC)(DA)(DC) (DA)(DA)(DA)(DA) (DA)(DT)(DA)(DG)(DG) (DT)(DC)(DA)(DG)(DT)(DC)(DT)(DG)(DT)(DC) (DT)(DG)(DG)(DC)(DT) (DA)(DG)(DT)(DT) (DC)(DT)(DG)(DT)(DA)(DC)(DT)(DT)(DG)(DC) (DA)(DG)(DA)(DC)(DA)(DC) (DA)(DG)(DG) (DG)(DC)(DA)(DT)(DG)(DT)(DG)(DG)(DG)(DG) (DT)(DT)(DC)(DC)(DT)(DA)(DT) (DT)(DT) |
-Macromolecule #6: DNA (162-MER)
Macromolecule | Name: DNA (162-MER) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 49.965957 KDa |
Sequence | String: (DA)(DA)(DA)(DT)(DA)(DG)(DG)(DA)(DA)(DC) (DC)(DC)(DC)(DA)(DC)(DA)(DT)(DG)(DC)(DC) (DC)(DT)(DG)(DT)(DG)(DT)(DC)(DT)(DG) (DC)(DA)(DA)(DG)(DT)(DA)(DC)(DA)(DG)(DA) (DA) (DC)(DT)(DA)(DG)(DC)(DC) ...String: (DA)(DA)(DA)(DT)(DA)(DG)(DG)(DA)(DA)(DC) (DC)(DC)(DC)(DA)(DC)(DA)(DT)(DG)(DC)(DC) (DC)(DT)(DG)(DT)(DG)(DT)(DC)(DT)(DG) (DC)(DA)(DA)(DG)(DT)(DA)(DC)(DA)(DG)(DA) (DA) (DC)(DT)(DA)(DG)(DC)(DC)(DA)(DG) (DA)(DC)(DA)(DG)(DA)(DC)(DT)(DG)(DA)(DC) (DC)(DT) (DA)(DT)(DT)(DT)(DT)(DT)(DG) (DT)(DG)(DA)(DG)(DG)(DG)(DG)(DA)(DA)(DT) (DC)(DG)(DG) (DG)(DA)(DA)(DG)(DT)(DA) (DT)(DC)(DC)(DA)(DT)(DT)(DG)(DC)(DT)(DA) (DA)(DG)(DA)(DC) (DT)(DC)(DA)(DG)(DC) (DA)(DA)(DT)(DG)(DC)(DT)(DG)(DC)(DA)(DA) (DC)(DT)(DC)(DT)(DC) (DA)(DG)(DC)(DA) (DA)(DC)(DC)(DA)(DG)(DC)(DT)(DG)(DA)(DA) (DG)(DA)(DT)(DC)(DA)(DG) (DC)(DA)(DG) (DC)(DC)(DG)(DA)(DG)(DA)(DG)(DG)(DC)(DC) (DC)(DT)(DG)(DC)(DA)(DC)(DC) (DT)(DA) |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.3 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 53.8 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.85 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 89583 |