Thiostrepton binds to malarial plastid rRNA

Barbara Clough*, Malcolm Strath, Peter Preiser, Paul Denny, Wilson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

86 Citations (Scopus)

Abstract

Binding of the thiazolyl peptide antibiotic thiostrepton to the GTPase domain of 23S rRNA involves a few crucial nucleotides, notably A1067 (E. coli). Small RNA transcripts were prepared corresponding to the GTPase domain of the plastid 23S rRNA and the two forms of cytosolic 28S rRNAs found in the human malaria parasite Plasmodium falciparum, as well as the plastid form of rRNA of the AIDS-related pathogen Toxoplasma gondii. Binding affinities of the wild type and mutated RNA sequences were as predicted; the malarial plastid sequence had by far the highest affinity, whereas that from toxoplasma did not bind thiostrepton.

Original languageEnglish
Pages (from-to)123-125
Number of pages3
JournalFEBS Letters
Volume406
Issue number1-2
DOIs
Publication statusPublished - 7 Apr 1997

Bibliographical note

Funding Information:
This work was supported by the UNPD/World Bank/WHO Special Programme for Research in Tropical Diseases (TDR) PD was supported by an MRC Studentship.

Keywords

  • GTPase domain
  • Malaria
  • rRNA
  • Thiostrepton
  • Toxoplasma

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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