|Entry||Database: EMDB / ID: EMD-0484|
|Title||Role of Era in Assembly and Homeostasis of the Ribosomal Small Subunit|
|Sample||Era+YjeQ-treated mature 30S subunit|
|Biological species||Escherichia coli (E. coli)|
|Method||single particle reconstruction / cryo EM / Resolution: 3.5 Å|
|Authors||Ortega J / Davis JH / Hao Y / Jahagirdar D / Thurlow B / Basu K / Jain N / Gomez-Blanco J / Britton RA / Vargas J / Guarne A / Woodson SA / Williamson JR / Ortega J|
|Funding support|| Canada, 1 items |
|Citation||Journal: Nucleic Acids Res. / Year: 2019|
Title: Role of Era in assembly and homeostasis of the ribosomal small subunit.
Authors: Aida Razi / Joseph H Davis / Yumeng Hao / Dushyant Jahagirdar / Brett Thurlow / Kaustuv Basu / Nikhil Jain / Josue Gomez-Blanco / Robert A Britton / Javier Vargas / Alba Guarné / Sarah A ...Authors: Aida Razi / Joseph H Davis / Yumeng Hao / Dushyant Jahagirdar / Brett Thurlow / Kaustuv Basu / Nikhil Jain / Josue Gomez-Blanco / Robert A Britton / Javier Vargas / Alba Guarné / Sarah A Woodson / James R Williamson / Joaquin Ortega /
Abstract: Assembly factors provide speed and directionality to the maturation process of the 30S subunit in bacteria. To gain a more precise understanding of how these proteins mediate 30S maturation, it is ...Assembly factors provide speed and directionality to the maturation process of the 30S subunit in bacteria. To gain a more precise understanding of how these proteins mediate 30S maturation, it is important to expand on studies of 30S assembly intermediates purified from bacterial strains lacking particular maturation factors. To reveal the role of the essential protein Era in the assembly of the 30S ribosomal subunit, we analyzed assembly intermediates that accumulated in Era-depleted Escherichia coli cells using quantitative mass spectrometry, high resolution cryo-electron microscopy and in-cell footprinting. Our combined approach allowed for visualization of the small subunit as it assembled and revealed that with the exception of key helices in the platform domain, all other 16S rRNA domains fold even in the absence of Era. Notably, the maturing particles did not stall while waiting for the platform domain to mature and instead re-routed their folding pathway to enable concerted maturation of other structural motifs spanning multiple rRNA domains. We also found that binding of Era to the mature 30S subunit destabilized helix 44 and the decoding center preventing binding of YjeQ, another assembly factor. This work establishes Era's role in ribosome assembly and suggests new roles in maintaining ribosome homeostasis.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_0484.map.gz / Format: CCP4 / Size: 107.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.073 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Era+YjeQ-treated mature 30S subunit
|Entire||Name: Era+YjeQ-treated mature 30S subunit|
Details: Mature 30S subunits exposed to Era and YjeQ proteins
Number of components: 1
-Component #1: protein, Era+YjeQ-treated mature 30S subunit
|Protein||Name: Era+YjeQ-treated mature 30S subunit|
Details: Mature 30S subunits exposed to Era and YjeQ proteins
Recombinant expression: No
|Mass||Theoretical: 900 kDa|
|Source||Species: Escherichia coli (E. coli) / Strain: K-12|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.5|
|Support film||5 mA|
|Vitrification||Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Temperature: 298.15 K / Humidity: 100 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 28 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 75000.0 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 1250.0 - 2750.0 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: FEI FALCON II (4k x 4k)|
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