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Mendelian and uniparental alterations in erythromycin binding by plastid ribosomes

Science (New York, N.Y.)
|November 1, 1971
PubMed

Insights

Erythromycin resistance in Chlamydomonas reinhardi chloroplast ribosomes was studied. Resistant mutants show altered antibiotic binding but normal ribosome structure, with varied genetic inheritance patterns.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Erythromycin is an antibiotic that targets bacterial and organelle ribosomes.
  • Chloroplast ribosomes in Chlamydomonas reinhardi are responsible for protein synthesis within the chloroplast.

Purpose of the Study:

  • To investigate the genetic basis of erythromycin resistance in Chlamydomonas reinhardi chloroplast ribosomes.
  • To characterize mutants with altered erythromycin binding affinity to chloroplast ribosomes.

Main Methods:

  • Isolation and characterization of erythromycin-resistant Chlamydomonas reinhardi mutants.
  • Analysis of ribosome sedimentation properties.
  • Genetic analysis to determine inheritance patterns.

Main Results:

  • Erythromycin specifically binds to the 52S subunit of Chlamydomonas reinhardi chloroplast ribosomes.
  • Isolated mutants exhibited resistance due to reduced ribosome affinity for erythromycin.
  • Ribosome sedimentation properties remained unchanged in resistant mutants compared to wild-type.
  • Mutants mapped to at least three distinct genetic loci.
  • Two loci displayed Mendelian inheritance, while one showed uniparental inheritance.

Conclusions:

  • Erythromycin resistance in Chlamydomonas reinhardi chloroplasts is mediated by alterations in ribosome-antibiotic interaction.
  • Genetic analysis reveals complex inheritance patterns for organelle antibiotic resistance.
  • The 52S ribosomal subunit is the primary target for erythromycin in Chlamydomonas reinhardi chloroplasts.

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