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Backbone and side chain NMR assignments for the ribosome maturation factor P (RimP) from Staphylococcus aureus

Natalia S Garaeva1,2, Aydar G Bikmullin1,2, Bulat F Fatkhullin2,3,4

  • 1Kazan Federal University, 18 Kremlevskaya, Kazan, Russian Federation, 420008.

Biomolecular NMR Assignments
|September 7, 2022
PubMed

Insights

The ribosomal maturation factor (RimP) from Staphylococcus aureus is crucial for 30S ribosome assembly. This study assigns its chemical shifts, revealing a structure that aids in understanding its role in ribosome maturation.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Ribosomal maturation factor (RimP) is essential for 30S ribosome assembly.
  • RimP's precise mechanism in stabilizing the central pseudoknot during ribosome maturation remains unclear.

Purpose of the Study:

  • To assign the 1H, 13C, and 15N chemical shifts for RimP from Staphylococcus aureus.
  • To elucidate the structural role of RimP in 30S ribosome biogenesis.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy for chemical shift assignment.
  • TALOS+ software for secondary structure prediction based on chemical shifts.

Main Results:

  • Complete assignment of backbone and side chain 1H, 13C, and 15N chemical shifts for Staphylococcus aureus RimP.
  • TALOS+ analysis predicted a secondary structure comprising eight β-strands and three α-helices with a specific topology (α1-β1-β2-α2-β3-α3-β4-β5-β6-β7-β8).

Conclusions:

  • The determined structure of RimP provides a foundation for understanding its function in ribosome assembly.
  • Integrated structural biology approaches including NMR, X-ray diffraction, and cryo-EM will enable further studies of RimP-ribosome complexes.
  • This research paves the way for developing targeted inhibitors of Staphylococcus aureus translation.
Keywords:
Protein NMRResonance assignmentRibosomeRibosome maturationRimPStaphylococcus aureusTEV protease

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