Abstract
The bacterial stringent response links nutrient starvation with the transcriptional control of genes. This process is initiated by the stringent factor RelA, which senses the presence of deacylated tRNA in the ribosome as a symptom of amino-acid starvation to synthesize the alarmone (p)ppGpp. Here we report a cryo-EM study of RelA bound to ribosomes bearing cognate, deacylated tRNA in the A-site. The data show that RelA on the ribosome stabilizes an unusual distorted form of the tRNA, with the acceptor arm making contact with RelA and far from its normal location in the peptidyl transferase centre.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding Sites
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Escherichia coli / chemistry
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Escherichia coli / metabolism
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / metabolism
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Molecular Docking Simulation
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Molecular Sequence Data
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RNA, Transfer / chemistry*
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RNA, Transfer / metabolism
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Ribosomal Proteins / chemistry
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Ribosomal Proteins / metabolism
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Ribosomes / metabolism*
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Transcription Factor RelA / chemistry*
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Transcription Factor RelA / metabolism
Substances
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Escherichia coli Proteins
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Ribosomal Proteins
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Transcription Factor RelA
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RNA, Transfer