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- EMDB-29316: Cryo-EM structure of RNase-untreated RESC-B in trypanosomal RNA e... -
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Open data
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Basic information
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Title | Cryo-EM structure of RNase-untreated RESC-B in trypanosomal RNA editing | ||||||||||||
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![]() | HEAT repeat / trypanosoma / RNA editing substrate binding complex / gRNA / RNA BINDING PROTEIN-RNA complex | ||||||||||||
Function / homology | ![]() regulation of mitochondrial mRNA stability / mitochondrial RNA modification / mitochondrial mRNA processing / RNA modification / ribonucleoprotein granule / mitochondrial mRNA editing complex / mitochondrial RNA processing / RNA metabolic process / cytoplasmic side of mitochondrial outer membrane / kinetoplast ...regulation of mitochondrial mRNA stability / mitochondrial RNA modification / mitochondrial mRNA processing / RNA modification / ribonucleoprotein granule / mitochondrial mRNA editing complex / mitochondrial RNA processing / RNA metabolic process / cytoplasmic side of mitochondrial outer membrane / kinetoplast / cytidine to uridine editing / mRNA stabilization / post-transcriptional regulation of gene expression / RNA processing / mitochondrial matrix / mRNA binding / mitochondrion / RNA binding / nucleus / cytoplasm Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||||||||
![]() | Liu S / Wang H / Li X / Zhang F / Lee JKJ / Li Z / Yu C / Zhao X / Hu JJ / Suematsu T ...Liu S / Wang H / Li X / Zhang F / Lee JKJ / Li Z / Yu C / Zhao X / Hu JJ / Suematsu T / Alvarez-Cabrera AL / Liu Q / Zhang L / Huang L / Aphasizheva I / Aphasizhev R / Zhou ZH | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of gRNA stabilization and mRNA recognition in trypanosomal RNA editing. Authors: Shiheng Liu / Hong Wang / Xiaorun Li / Fan Zhang / Jane K J Lee / Zihang Li / Clinton Yu / Jason J Hu / Xiaojing Zhao / Takuma Suematsu / Ana L Alvarez-Cabrera / Qiushi Liu / Liye Zhang / ...Authors: Shiheng Liu / Hong Wang / Xiaorun Li / Fan Zhang / Jane K J Lee / Zihang Li / Clinton Yu / Jason J Hu / Xiaojing Zhao / Takuma Suematsu / Ana L Alvarez-Cabrera / Qiushi Liu / Liye Zhang / Lan Huang / Inna Aphasizheva / Ruslan Aphasizhev / Z Hong Zhou / ![]() ![]() Abstract: In , the editosome, composed of RNA-editing substrate-binding complex (RESC) and RNA-editing catalytic complex (RECC), orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial ...In , the editosome, composed of RNA-editing substrate-binding complex (RESC) and RNA-editing catalytic complex (RECC), orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial transcripts into messenger RNAs (mRNAs). The mechanism of information transfer from gRNA to mRNA is unclear owing to a lack of high-resolution structures for these complexes. With cryo-electron microscopy and functional studies, we have captured gRNA-stabilizing RESC-A and gRNA-mRNA-binding RESC-B and RESC-C particles. RESC-A sequesters gRNA termini, thus promoting hairpin formation and blocking mRNA access. The conversion of RESC-A into RESC-B or -C unfolds gRNA and allows mRNA selection. The ensuing gRNA-mRNA duplex protrudes from RESC-B, likely exposing editing sites to RECC-catalyzed cleavage, uridine insertion or deletion, and ligation. Our work reveals a remodeling event facilitating gRNA-mRNA hybridization and assembly of a macromolecular substrate for the editosome's catalytic modality. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 398.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 28.7 KB 28.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 15.9 KB | Display | ![]() |
Images | ![]() | 92.7 KB | ||
Filedesc metadata | ![]() | 9.1 KB | ||
Others | ![]() ![]() | 391.1 MB 391.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8fnkMC ![]() 8fn4C ![]() 8fn6C ![]() 8fncC ![]() 8fnfC ![]() 8fniC 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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Map
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Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_29316_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_29316_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
+Entire : RESC5-tagged isolate without RNase treatment
+Supramolecule #1: RESC5-tagged isolate without RNase treatment
+Macromolecule #1: mRNA
+Macromolecule #2: gRNA
+Macromolecule #3: RNA-editing substrate-binding complex protein 5 (RESC5)
+Macromolecule #4: RNA-editing substrate-binding complex protein 6 (RESC6)
+Macromolecule #5: RNA-editing substrate-binding complex protein 7 (RESC7)
+Macromolecule #6: RNA-editing substrate-binding complex protein 8 (RESC8)
+Macromolecule #7: RNA-editing substrate-binding complex protein 9 (RESC9)
+Macromolecule #8: RNA-editing substrate-binding complex protein 10 (RESC10)
+Macromolecule #9: RNA-editing substrate-binding complex protein 11 (RESC11)
+Macromolecule #10: RNA-editing substrate-binding complex protein 13 (RESC13)
+Macromolecule #11: RNA-editing substrate-binding complex protein 14 (RESC14)
-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: 7.5 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281.15 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: GATAN K3 (6k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |