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Principles of human pre-60S biogenesis.

Arnaud Vanden Broeck1, Sebastian Klinge1

  • 1Laboratory of Protein and Nucleic Acid Chemistry, The Rockefeller University, New York, NY 10065, USA.

Science (New York, N.Y.)
|July 6, 2023
PubMed
Summary

Researchers visualized human large ribosomal subunit assembly intermediates using cryo-electron microscopy. This reveals how assembly factors and nucleotide hydrolysis establish functional RNA centers during ribosome biogenesis.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • Human large ribosomal subunit (60S) biogenesis involves intricate assembly of RNA and proteins.
  • The precise mechanisms by which assembly factors establish functional RNA centers remain largely unknown.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying human 60S ribosomal subunit biogenesis.
  • To visualize the structural intermediates of pre-60S particle assembly.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine structures of human nucleolar and nuclear pre-60S assembly intermediates.
  • High-resolution structures (2.5–3.2 angstroms) were obtained for multiple assembly states.

Main Results:

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  • Structural snapshots reveal how protein interaction hubs anchor assembly factors to pre-60S particles.
  • Guanosine triphosphatases (GTPases) and adenosine triphosphatases (ATPases) were shown to couple nucleotide hydrolysis to functional center installation.
  • Nuclear stages illustrate the rixosome complex coupling RNA conformational changes with RNA processing.

Conclusions:

  • The study provides a detailed structural basis for understanding human ribosome biogenesis.
  • These findings offer insights into the coordinated action of assembly factors, nucleotide hydrolysis, and RNA processing machinery.