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Open data
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Basic information
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Title | Bacterial transcription termination factor Rho G150D mutant | |||||||||
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![]() | Rho / termination / TRANSCRIPTION | |||||||||
Function / homology | ![]() ATP-dependent activity, acting on RNA / helicase activity / DNA-templated transcription termination / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / ATP hydrolysis activity / RNA binding / ATP binding / identical protein binding / membrane / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Said N / Hilal T / Wahl MC | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Transcription termination factor ρ polymerizes under stress. Authors: Bing Wang / Nelly Said / Tarek Hilal / Mark Finazzo / Markus C Wahl / Irina Artsimovitch / ![]() ![]() Abstract: Bacterial RNA helicase ρ is a genome sentinel that terminates synthesis of damaged and junk RNAs that are not translated by the ribosome. Co-transcriptional RNA surveillance by ρ is essential for ...Bacterial RNA helicase ρ is a genome sentinel that terminates synthesis of damaged and junk RNAs that are not translated by the ribosome. Co-transcriptional RNA surveillance by ρ is essential for quality control of the transcriptome during optimal growth. However, it is unclear how bacteria protect their RNAs from overzealous ρ during dormancy or stress, conditions common in natural habitats. Here we used cryogenic electron microscopy, biochemical, and genetic approaches to show that residue substitutions, ADP, or ppGpp promote hyper-oligomerization of ρ. Our results demonstrate that nucleotides bound at subunit interfaces control ρ switching from active hexamers to inactive higher-order oligomers and extended filaments. Polymers formed upon exposure to antibiotics or ppGpp disassemble when stress is relieved, thereby directly linking termination activity to cellular physiology. Inactivation of ρ through hyper-oligomerization is a regulatory strategy shared by RNA polymerases, ribosomes, and metabolic enzymes across all life. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 52.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.8 KB 15.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.8 KB | Display | ![]() |
Images | ![]() | 86.9 KB | ||
Filedesc metadata | ![]() | 5.8 KB | ||
Others | ![]() ![]() | 200.3 MB 200.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8q3pMC ![]() 8q3nC ![]() 8q3oC ![]() 8q3qC 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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Voxel size | X=Y=Z: 0.832 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_18132_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_18132_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Filament of Rho mutant G150D
Entire | Name: Filament of Rho mutant G150D |
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Components |
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-Supramolecule #1: Filament of Rho mutant G150D
Supramolecule | Name: Filament of Rho mutant G150D / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Transcription termination factor Rho
Macromolecule | Name: Transcription termination factor Rho / type: protein_or_peptide / ID: 1 / Number of copies: 18 / Enantiomer: LEVO EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 48.616809 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGHMNLTELK NTPVSELITL GENMGLENLA RMRKQDIIFA ILKQHAKSGE DIFGDGVLEI LQDGFGFLRS ADSSYLAGPD DIYVSPSQI RRFNLRTGDT ISGKIRPPKE GERYFALLKV NEVNFDKPEN ARNKILFENL TPLHANSRLR MERDNGSTED L TARVLDLA ...String: MGHMNLTELK NTPVSELITL GENMGLENLA RMRKQDIIFA ILKQHAKSGE DIFGDGVLEI LQDGFGFLRS ADSSYLAGPD DIYVSPSQI RRFNLRTGDT ISGKIRPPKE GERYFALLKV NEVNFDKPEN ARNKILFENL TPLHANSRLR MERDNGSTED L TARVLDLA SPIGRGQRGL IVAPPKAGKT MLLQNIAQSI AYNHPDCVLM VLLIDERPEE VTEMQRLVKG EVVASTFDEP AS RHVQVAE MVIEKAKRLV EHKKDVIILL DSITRLARAY NTVVPASGKV LTGGVDANAL HRPKRFFGAA RNVEEGGSLT IIA TALIDT GSKMDEVIYE EFKGTGNMEL HLSRKIAEKR VFPAIDYNRS GTRKEELLTT QEELQKMWIL RKIIHPMGEI DAME FLINK LAMTKTNDDF FEMMKRSGHH HHHHHH UniProtKB: Transcription termination factor Rho |
-Macromolecule #2: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 18 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #3: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 18 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 2.4 mg/mL |
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Buffer | pH: 7.6 |
Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 2511 / Average exposure time: 40.57 sec. / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.9 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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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: RIGID BODY FIT / Overall B value: 96.4 |
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Output model | ![]() PDB-8q3p: |