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Structural basis of ribosomal 30S subunit degradation by RNase R.

Lyudmila Dimitrova-Paternoga1, Sergo Kasvandik2, Bertrand Beckert3

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|February 7, 2024
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Ribonuclease R (RNase R) degrades small ribosomal 30S subunits by binding to the platform and overcoming a structural roadblock via head rearrangement. This enzyme alone can fully degrade 30S subunits, revealing a dynamic mechanism for ribosome turnover.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Ribosome production and turnover are crucial for cellular energy and protein synthesis.
  • Understanding ribosome degradation is essential, yet structural insights have been limited.

Purpose of the Study:

  • To elucidate the structural mechanism of small ribosomal 30S subunit degradation by ribonuclease R (RNase R).

Main Methods:

  • Native structural analysis of RNase R-30S subunit degradation intermediates.
  • In vitro degradation assays.

Main Results:

  • RNase R initially binds the 30S platform, degrading key sequences.
  • A structural rearrangement of the 30S head, involving protein loss, overcomes a degradation roadblock.
  • RNase R relocates to the decoding site using its N-terminal domain as an anchor.

Conclusions:

  • RNase R employs a dynamic, site-switching mechanism to degrade 30S subunits.
  • The enzyme is sufficient for complete 30S subunit degradation, providing a mechanistic basis for ribosome turnover.