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- EMDB-13713: CryoEM structure of E.coli RNA polymerase elongation complex boun... -
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Open data
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Basic information
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Title | CryoEM structure of E.coli RNA polymerase elongation complex bound to NusA and NusG (the consensus NusA-NusG-EC) | ||||||||||||
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Function / homology | ![]() bacterial-type RNA polymerase core enzyme binding / transcription elongation-coupled chromatin remodeling / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Zhu C / Guo X / Weixlbaumer A | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Transcription factors modulate RNA polymerase conformational equilibrium. Authors: Chengjin Zhu / Xieyang Guo / Philippe Dumas / Maria Takacs / Mo'men Abdelkareem / Arnaud Vanden Broeck / Charlotte Saint-André / Gabor Papai / Corinne Crucifix / Julio Ortiz / Albert Weixlbaumer / ![]() ![]() ![]() Abstract: RNA polymerase (RNAP) frequently pauses during the transcription of DNA to RNA to regulate gene expression. Transcription factors NusA and NusG modulate pausing, have opposing roles, but can bind ...RNA polymerase (RNAP) frequently pauses during the transcription of DNA to RNA to regulate gene expression. Transcription factors NusA and NusG modulate pausing, have opposing roles, but can bind RNAP simultaneously. Here we report cryo-EM reconstructions of Escherichia coli RNAP bound to NusG, or NusA, or both. RNAP conformational changes, referred to as swivelling, correlate with transcriptional pausing. NusA facilitates RNAP swivelling to further increase pausing, while NusG counteracts this role. Their structural effects are consistent with biochemical results on two categories of transcriptional pauses. In addition, the structures suggest a cooperative mechanism of NusA and NusG during Rho-mediated transcription termination. Our results provide a structural rationale for the stochastic nature of pausing and termination and how NusA and NusG can modulate it. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 79.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 25.6 KB 25.6 KB | Display Display | ![]() |
Images | ![]() | 120.7 KB | ||
Others | ![]() ![]() | 42.1 MB 75.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7py5MC ![]() 7py0C ![]() 7py1C ![]() 7py3C ![]() 7py6C ![]() 7py7C ![]() 7py8C ![]() 7pyjC ![]() 7pykC ![]() 7q0jC ![]() 7q0kC 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: 1.09 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
File | emd_13713_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: #2
File | emd_13713_additional_2.map | ||||||||||||
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Density Histograms |
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Sample components
+Entire : NusA and NusG elongation complex (consensus)
+Supramolecule #1: NusA and NusG elongation complex (consensus)
+Macromolecule #1: ntDNA
+Macromolecule #2: tDNA
+Macromolecule #3: RNA
+Macromolecule #4: DNA-directed RNA polymerase subunit alpha
+Macromolecule #5: DNA-directed RNA polymerase subunit beta
+Macromolecule #6: DNA-directed RNA polymerase subunit beta'
+Macromolecule #7: DNA-directed RNA polymerase subunit omega
+Macromolecule #8: Transcription termination/antitermination protein NusG
+Macromolecule #9: Transcription termination/antitermination protein NusA
+Macromolecule #10: MAGNESIUM ION
+Macromolecule #11: ZINC ION
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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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: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
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Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 259835 |