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Sequence-dependent elongation dynamics on macrolide-bound ribosomes.

Magnus Johansson1, Jin Chen2, Albert Tsai2

  • 1Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.

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|May 20, 2014
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Macrolide antibiotics interact dynamically with nascent peptides within the ribosomal exit tunnel, influencing translation rather than simply blocking it. These drug-peptide interactions dictate whether ribosomes stall or continue translation.

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Area of Science:

  • Molecular Biology
  • Microbiology
  • Biochemistry

Background:

  • The traditional model of macrolide antibiotics acting as simple plugs in the ribosomal nascent peptide exit tunnel (NPET) is being re-evaluated.
  • Emerging evidence suggests a more complex, heterogeneous mechanism involving drug-peptide interactions.

Purpose of the Study:

  • To investigate the dynamic processes of macrolide antibiotic interaction with translating ribosomes.
  • To understand how drug-peptide interactions affect ribosomal elongation dynamics and the fate of protein synthesis.

Main Methods:

  • Single-molecule tracking of elongating ribosomes.
  • Inhibition of elongation using erythromycin with various nascent chains (ErmCL, H-NS).
  • Analysis of translation dynamics and pausing events.

Main Results:

  • Peptide sequence-specific alterations in translation elongation dynamics were observed with macrolide-obstructed NPET.
  • Erythromycin did not generally inhibit elongation rates but caused abrupt stalls or pauses.
  • Nascent chain-dependent elongation pausing pathways in the presence of macrolides influenced ribosome fate (stalling vs. readthrough).

Conclusions:

  • Macrolide antibiotic action is a complex, dynamic process influenced by nascent peptide sequence.
  • Drug-peptide interactions, not just physical obstruction, govern ribosome behavior during macrolide inhibition.
  • This provides a new perspective on macrolide antibiotic mechanisms and resistance.