IndraLab

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Thiostrepton inhibits RELA. 6 / 6
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"We show that in a biochemical system from purified E. coli components, the antibiotic thiostrepton efficiently inhibits RelA activation by the A-site tRNA."
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"We have shown that thiostrepton specifically inhibits RelA activation by the A-site tRNA and has no effect on RelA activated by 70S alone, whereas EF-G is inhibited equally efficiently regardless of the presence or absence of A-site tRNA (XREF_FIG)."
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"The cyclic peptide thiostrepton is an efficient inhibitor of both translational GTPases, targeting initiation factor IF2 and elongation factors EF-Tu and EF-G on the ribosome, and E. coli RelA."
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"Thiostrepton specifically inhibits RelA activation by A-site deacylated tRNA while not affecting RelA activation by the ribosome itself."
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"Next, we tested whether the dependence of RelA inhibition by thiostrepton on the presence of A-site deacylated tRNA, the ultimate inducer of the enzyme 's enzymatic activity and a key factor in promoting RelA binding to the ribosome, is specific to this antibiotic."
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"A-site tRNA dependent inhibition of RelA by thiostrepton."
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