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TitleThe ribosome triggers the stringent response by RelA via a highly distorted tRNA.
Journal, issue, pagesEMBO Rep, Vol. 14, Issue 9, Page 811-816, Year 2013
Publish dateJul 23, 2013
AuthorsXabier Agirrezabala / Israel S Fernández / Ann C Kelley / David Gil Cartón / Venki Ramakrishnan / Mikel Valle /
PubMed AbstractThe 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 ...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.
External linksEMBO Rep / PubMed:23877429 / PubMed Central
MethodsEM (single particle)
Resolution14.5 Å
Structure data

EMDB-2373:
ribosome-RelA complex
Method: EM (single particle) / Resolution: 14.5 Å

Source
  • Thermus thermophilus (bacteria)
  • Escherichia coli (E. coli)

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