Thiostrepton binds to malarial plastid rRNA

被引:73
作者
Clough, B
Strath, M
Preiser, P
Denny, P
Wilson, I
机构
[1] Natl. Institute for Medical Research, Mill Hill
关键词
malaria; toxoplasma; thiostrepton; GTPase domain; rRNA;
D O I
10.1016/S0014-5793(97)00241-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:123 / 125
页数:3
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