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Conformational changes in the ribosome induced by translational miscoding agents

O Jerinic1, S Joseph

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0314, USA.

Insights

Translational miscoding agents like aminoglycosides alter ribosome structure, impacting protein synthesis accuracy. This study confirms these structural changes correlate with their effects in living organisms.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Ribosomes translate mRNA to proteins, a crucial process for life.
  • Translational fidelity is vital; miscoding agents compromise this accuracy.
  • Aminoglycosides are miscoding agents known to affect ribosome structure and translation.

Purpose of the Study:

  • To investigate how miscoding agents induce conformational changes in Escherichia coli ribosomes.
  • To correlate in vitro observed structural changes with in vivo phenotypes.

Main Methods:

  • Utilized a toeprinting assay to detect structural alterations in ribosomes.
  • Tested various aminoglycosides (streptomycin, neomycin, kanamycin, gentamycin, hygromycin B), miscoding agents (viomycin, ethanol), and non-miscoding antibiotics (tetracycline, chloramphenicol, erythromycin, fusidic acid, spectinomycin).
  • Examined ribosomes from streptomycin-resistant and streptomycin-dependent strains.

Main Results:

  • Streptomycin, neomycin, kanamycin, gentamycin, and hygromycin B induced conformational changes in E. coli ribosomes.
  • Other miscoding agents (viomycin, ethanol) also caused similar structural changes.
  • Non-miscoding antibiotics did not induce these conformational changes.
  • Ribosomes from streptomycin-resistant or dependent strains did not exhibit changes with streptomycin.

Conclusions:

  • Miscoding agents trigger specific conformational changes in bacterial ribosomes.
  • These structural alterations are linked to the observed in vivo effects of miscoding agents.
  • The findings provide a molecular basis for understanding aminoglycoside action.

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