+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-19641 | |||||||||
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Title | YlmH bound to stalled 50S subunits with RqcH and PtRNA | |||||||||
Map data | ||||||||||
Sample |
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Keywords | LSU / 50S / RQC / YlmH / RIBOSOME / RqcH | |||||||||
Function / homology | Function and homology information RQC complex / positive regulation of rRNA processing / nucleoid / ribosomal large subunit binding / rescue of stalled ribosome / rRNA processing / ribosomal small subunit biogenesis / large ribosomal subunit / small ribosomal subunit / 5S rRNA binding ...RQC complex / positive regulation of rRNA processing / nucleoid / ribosomal large subunit binding / rescue of stalled ribosome / rRNA processing / ribosomal small subunit biogenesis / large ribosomal subunit / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / mRNA binding / DNA binding / RNA binding / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Bacillus subtilis subsp. subtilis str. 168 (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Paternoga H / Wilson DN | |||||||||
Funding support | Germany, 1 items
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Citation | Journal: Nucleic Acids Res / Year: 2024 Title: A role for the S4-domain containing protein YlmH in ribosome-associated quality control in Bacillus subtilis. Authors: Hiraku Takada / Helge Paternoga / Keigo Fujiwara / Jose A Nakamoto / Esther N Park / Lyudmila Dimitrova-Paternoga / Bertrand Beckert / Merilin Saarma / Tanel Tenson / Allen R Buskirk / Gemma ...Authors: Hiraku Takada / Helge Paternoga / Keigo Fujiwara / Jose A Nakamoto / Esther N Park / Lyudmila Dimitrova-Paternoga / Bertrand Beckert / Merilin Saarma / Tanel Tenson / Allen R Buskirk / Gemma C Atkinson / Shinobu Chiba / Daniel N Wilson / Vasili Hauryliuk / Abstract: Ribosomes trapped on mRNAs during protein synthesis need to be rescued for the cell to survive. The most ubiquitous bacterial ribosome rescue pathway is trans-translation mediated by tmRNA and SmpB. ...Ribosomes trapped on mRNAs during protein synthesis need to be rescued for the cell to survive. The most ubiquitous bacterial ribosome rescue pathway is trans-translation mediated by tmRNA and SmpB. Genetic inactivation of trans-translation can be lethal, unless ribosomes are rescued by ArfA or ArfB alternative rescue factors or the ribosome-associated quality control (RQC) system, which in Bacillus subtilis involves MutS2, RqcH, RqcP and Pth. Using transposon sequencing in a trans-translation-incompetent B. subtilis strain we identify a poorly characterized S4-domain-containing protein YlmH as a novel potential RQC factor. Cryo-EM structures reveal that YlmH binds peptidyl-tRNA-50S complexes in a position analogous to that of S4-domain-containing protein RqcP, and that, similarly to RqcP, YlmH can co-habit with RqcH. Consistently, we show that YlmH can assume the role of RqcP in RQC by facilitating the addition of poly-alanine tails to truncated nascent polypeptides. While in B. subtilis the function of YlmH is redundant with RqcP, our taxonomic analysis reveals that in multiple bacterial phyla RqcP is absent, while YlmH and RqcH are present, suggesting that in these species YlmH plays a central role in the RQC. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_19641.map.gz | 36.3 MB | EMDB map data format | |
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Header (meta data) | emd-19641-v30.xml emd-19641.xml | 51.4 KB 51.4 KB | Display Display | EMDB header |
Images | emd_19641.png | 101.3 KB | ||
Masks | emd_19641_msk_1.map | 216 MB | Mask map | |
Filedesc metadata | emd-19641.cif.gz | 11.4 KB | ||
Others | emd_19641_additional_1.map.gz emd_19641_half_map_1.map.gz emd_19641_half_map_2.map.gz | 171.4 MB 171.7 MB 171.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-19641 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-19641 | HTTPS FTP |
-Validation report
Summary document | emd_19641_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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Full document | emd_19641_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | emd_19641_validation.xml.gz | 15.6 KB | Display | |
Data in CIF | emd_19641_validation.cif.gz | 18.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19641 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19641 | HTTPS FTP |
-Related structure data
Related structure data | 8s1uMC 8s1pC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_19641.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.8 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_19641_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: #1
File | emd_19641_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_19641_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_19641_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : 50S ribosomal subunit with stalled P-tRNA-nascent chain, bound by YlmH
+Supramolecule #1: 50S ribosomal subunit with stalled P-tRNA-nascent chain, bound by YlmH
+Macromolecule #1: P-tRNA
+Macromolecule #8: 5S rRNA
+Macromolecule #32: 23S rRNA
+Macromolecule #2: 50S ribosomal protein L32
+Macromolecule #3: 50S ribosomal protein L33 1
+Macromolecule #4: 50S ribosomal protein L34
+Macromolecule #5: 50S ribosomal protein L35
+Macromolecule #6: 50S ribosomal protein L36
+Macromolecule #7: 50S ribosomal protein L31
+Macromolecule #9: 50S ribosomal protein L2
+Macromolecule #10: 50S ribosomal protein L3
+Macromolecule #11: 50S ribosomal protein L4
+Macromolecule #12: 50S ribosomal protein L5
+Macromolecule #13: Large ribosomal subunit protein uL6
+Macromolecule #14: 50S ribosomal protein L13
+Macromolecule #15: 50S ribosomal protein L14
+Macromolecule #16: 50S ribosomal protein L15
+Macromolecule #17: 50S ribosomal protein L16
+Macromolecule #18: 50S ribosomal protein L17
+Macromolecule #19: 50S ribosomal protein L18
+Macromolecule #20: 50S ribosomal protein L19
+Macromolecule #21: Large ribosomal subunit protein bL20
+Macromolecule #22: 50S ribosomal protein L21
+Macromolecule #23: 50S ribosomal protein L22
+Macromolecule #24: Large ribosomal subunit protein uL23
+Macromolecule #25: 50S ribosomal protein L24
+Macromolecule #26: Putative RNA-binding protein YlmH
+Macromolecule #27: Large ribosomal subunit protein bL27
+Macromolecule #28: 50S ribosomal protein L28
+Macromolecule #29: 50S ribosomal protein L29
+Macromolecule #30: Large ribosomal subunit protein uL30
+Macromolecule #31: Rqc2 homolog RqcH
+Macromolecule #33: POTASSIUM ION
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Grid | Model: Quantifoil R3/3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 3 |
Vitrification | Cryogen name: ETHANE-PROPANE / Chamber humidity: 100 % |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 0.9 µm / Nominal defocus min: 0.4 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |