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Open data
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Basic information
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Title | Structure of MuvB complex | |||||||||
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![]() | Quiescence / transcription / cell cycle | |||||||||
Function / homology | ![]() Myb complex / CAF-1 complex / NuRD complex / NURF complex / regulation of cell fate specification / negative regulation of stem cell population maintenance / DNA replication-dependent chromatin assembly / Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 / ESC/E(Z) complex / regulation of stem cell differentiation ...Myb complex / CAF-1 complex / NuRD complex / NURF complex / regulation of cell fate specification / negative regulation of stem cell population maintenance / DNA replication-dependent chromatin assembly / Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 / ESC/E(Z) complex / regulation of stem cell differentiation / Polo-like kinase mediated events / Transcription of E2F targets under negative control by DREAM complex / DNA biosynthetic process / ATPase complex / Sin3-type complex / G1/S-Specific Transcription / positive regulation of stem cell population maintenance / Transcriptional Regulation by E2F6 / RNA Polymerase I Transcription Initiation / histone deacetylase complex / G0 and Early G1 / Cyclin E associated events during G1/S transition / Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 / Cyclin A:Cdk2-associated events at S phase entry / Regulation of TP53 Activity through Acetylation / Deposition of new CENPA-containing nucleosomes at the centromere / transcription repressor complex / negative regulation of cell migration / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / Regulation of PTEN gene transcription / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / HDACs deacetylate histones / negative regulation of transforming growth factor beta receptor signaling pathway / brain development / PKMTs methylate histone lysines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / histone deacetylase binding / HCMV Early Events / nucleosome assembly / Oxidative Stress Induced Senescence / histone binding / Potential therapeutics for SARS / chromosome, telomeric region / DNA replication / regulation of cell cycle / chromatin remodeling / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of cell population proliferation / DNA repair / negative regulation of DNA-templated transcription / DNA-templated transcription / regulation of transcription by RNA polymerase II / regulation of DNA-templated transcription / chromatin / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Koliopoulos MG / Alfieri C | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of a nucleosome-bound MuvB transcription factor complex reveals DNA remodelling. Authors: Marios G Koliopoulos / Reyhan Muhammad / Theodoros I Roumeliotis / Fabienne Beuron / Jyoti S Choudhary / Claudio Alfieri / ![]() Abstract: Genes encoding the core cell cycle machinery are transcriptionally regulated by the MuvB family of protein complexes in a cell cycle-specific manner. Complexes of MuvB with the transcription factors ...Genes encoding the core cell cycle machinery are transcriptionally regulated by the MuvB family of protein complexes in a cell cycle-specific manner. Complexes of MuvB with the transcription factors B-MYB and FOXM1 activate mitotic genes during cell proliferation. The mechanisms of transcriptional regulation by these complexes are still poorly characterised. Here, we combine biochemical analysis and in vitro reconstitution, with structural analysis by cryo-electron microscopy and cross-linking mass spectrometry, to functionally examine these complexes. We find that the MuvB:B-MYB complex binds and remodels nucleosomes, thereby exposing nucleosomal DNA. This remodelling activity is supported by B-MYB which directly binds the remodelled DNA. Given the remodelling activity on the nucleosome, we propose that the MuvB:B-MYB complex functions as a pioneer transcription factor complex. In this work, we rationalise prior biochemical and cellular studies and provide a molecular framework of interactions on a protein complex that is key for cell cycle regulation. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 2.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.8 KB 14.8 KB | Display Display | ![]() |
Images | ![]() | 99 KB | ||
Filedesc metadata | ![]() | 6.4 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 324.8 KB | Display | ![]() |
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Full document | ![]() | 324.4 KB | Display | |
Data in XML | ![]() | 5.8 KB | Display | |
Data in CIF | ![]() | 6.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7r1dMC 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
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.134 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 : MuvB complex
Entire | Name: MuvB complex |
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Components |
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-Supramolecule #1: MuvB complex
Supramolecule | Name: MuvB complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 180 KDa |
-Macromolecule #1: Protein lin-9 homolog
Macromolecule | Name: Protein lin-9 homolog / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 62.03566 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MAELDQLPDE SSSAKALVSL KEGSLSNTWN EKYSSLQKTP VWKGRNTSSA VEMPFRNSKR SRLFSDEDDR QINTRSPKRN QRVAMVPQK FTATMSTPDK KASQKIGFRL RNLLKLPKAH KWCIYEWFYS NIDKPLFEGD NDFCVCLKES FPNLKTRKLT R VEWGKIRR ...String: MAELDQLPDE SSSAKALVSL KEGSLSNTWN EKYSSLQKTP VWKGRNTSSA VEMPFRNSKR SRLFSDEDDR QINTRSPKRN QRVAMVPQK FTATMSTPDK KASQKIGFRL RNLLKLPKAH KWCIYEWFYS NIDKPLFEGD NDFCVCLKES FPNLKTRKLT R VEWGKIRR LMGKPRRCSS AFFEEERSAL KQKRQKIRLL QQRKVADVSQ FKDLPDEIPL PLVIGTKVTA RLRGVHDGLF TG QIDAVDT LNATYRVTFD RTGLGTHTIP DYEVLSNEPH ETMPIAAFGQ KQRPSRFFMT PPRLHYTPPL QSPIIDNDPL LGQ SPWRSK ISGSDTETLG GFPVEFLIQV TRLSKILMIK KEHIKKLREM NTEAEKLKSY SMPISIEFQR RYATIVLELE QLNK DLNKV LHKVQQYCYE LAPDQGLQPA DQPTDMRRRC EEEAQEIVRH ANSSTGQPCV ENENLTDLIS RLTAILLQIK CLAEG GDLN SFEFKSLTDS LNDIKSTIDA SNISCFQNNV EIHVAHIQSG LSQMGNLHAF AANNTNRD UniProtKB: Protein lin-9 homolog |
-Macromolecule #2: Histone-binding protein RBBP4
Macromolecule | Name: Histone-binding protein RBBP4 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 47.709527 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPEGKD FSIHRLVLGT HTSDEQNHLV IASVQLPND DAQFDASHYD SEKGEFGGFG SVSGKIEIEI KINHEGEVNR ARYMPQNPCI IATKTPSSDV LVFDYTKHPS K PDPSGECN ...String: MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPEGKD FSIHRLVLGT HTSDEQNHLV IASVQLPND DAQFDASHYD SEKGEFGGFG SVSGKIEIEI KINHEGEVNR ARYMPQNPCI IATKTPSSDV LVFDYTKHPS K PDPSGECN PDLRLRGHQK EGYGLSWNPN LSGHLLSASD DHTICLWDIS AVPKEGKVVD AKTIFTGHTA VVEDVSWHLL HE SLFGSVA DDQKLMIWDT RSNNTSKPSH SVDAHTAEVN CLSFNPYSEF ILATGSADKT VALWDLRNLK LKLHSFESHK DEI FQVQWS PHNETILASS GTDRRLNVWD LSKIGEEQSP EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWVICSVSED NIMQ VWQMA ENIYNDEDPE GSVDPEGQGS UniProtKB: Histone-binding protein RBBP4 |
-Macromolecule #3: Protein lin-37 homolog
Macromolecule | Name: Protein lin-37 homolog / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 29.37524 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MFPVKVKVEK SELEMAKARN QLDAVLQCLL EKSHMDRERL DEEAGKTPSD THNKDCSIAA TGKRPSARFP HQRRKKRREM DDGLAEGGP QRSNTYVIKL FDRSVDLAQF SENTPLYPIC RAWMRNSPSV RERECSPSSP LPPLPEDEEG SEVTNSKSRD V YKLPPPTP ...String: MFPVKVKVEK SELEMAKARN QLDAVLQCLL EKSHMDRERL DEEAGKTPSD THNKDCSIAA TGKRPSARFP HQRRKKRREM DDGLAEGGP QRSNTYVIKL FDRSVDLAQF SENTPLYPIC RAWMRNSPSV RERECSPSSP LPPLPEDEEG SEVTNSKSRD V YKLPPPTP PGPPGDACRS RIPSPLQPEM QGTPDDEPSE PEPSPSTLIY RNMQRWKRIR QRWKEASHRN QLRYSESMKI LR EMYERQG SALEVLFQ UniProtKB: Protein lin-37 homolog |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Grid | Material: COPPER |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.6 µm |