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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
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SrmB Rescues Trapped Ribosome Assembly Intermediates.

Jessica N Rabuck-Gibbons1, Anna M Popova2, Emily M Greene2

  • 1Department of Integrative, Structural and Computational Biology, The Scripps Research Institute, 10550 N Torrey Pines Road, La Jolla, CA, 92037, USA; Laboratory of Genetics and Helmsley Center for Genomic Medicine, The Salk Institute for Biological Studies, 10010 N Torrey Pines Road, La Jolla, CA, 92037, USA.

Journal of Molecular Biology
|December 27, 2019
PubMed
Summary

DEAD-box helicase SrmB is crucial for early ribosome biogenesis. Its absence causes severe assembly defects in 40S ribosomal intermediates, impacting key functional sites.

Keywords:
Cryo-electron microscopyDEAD-box helicaseQuantitative mass spectrometryRibosome biogenesisSrmB

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cellular Biology

Background:

  • Ribosome biogenesis is essential for cell function and involves complex assembly pathways.
  • RNA helicases regulate ribosome assembly, but their specific roles and interactions with intermediates remain largely unknown.
  • SrmB, a DEAD-box helicase, functions early in ribosome assembly, yet its precise mechanism is poorly understood.

Purpose of the Study:

  • To investigate the role of SrmB in 40S ribosome assembly.
  • To elucidate the structural and compositional changes in ribosomal intermediates lacking SrmB.
  • To propose mechanisms for SrmB's function in guiding ribosome assembly.

Main Methods:

  • Quantitative mass spectrometry to analyze protein inventory.
  • Cryo-electron microscopy to determine structures of 40S ribosomal intermediates.
  • Comparative analysis of wild-type and SrmB-deletion mutant cells.

Main Results:

  • Deletion of SrmB did not affect its binding site but caused significant assembly defects.
  • Key functional regions of the 40S subunit, including the peptidyl transferase center and uL7/12 stalk, were impaired.
  • Specific contact sites with the 30S subunit also exhibited assembly defects.

Conclusions:

  • SrmB is essential for overcoming kinetic traps during early 50S ribosome assembly.
  • The absence of SrmB leads to misassembly of critical functional centers within the 40S subunit.
  • Proposed mechanisms suggest SrmB actively guides the conformational maturation of assembling ribosomes.