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-Structure paper
Title | The ribosome triggers the stringent response by RelA via a highly distorted tRNA. |
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Journal, issue, pages | EMBO Rep, Vol. 14, Issue 9, Page 811-816, Year 2013 |
Publish date | Jul 23, 2013 |
Authors | Xabier Agirrezabala / Israel S Fernández / Ann C Kelley / David Gil Cartón / Venki Ramakrishnan / Mikel Valle / |
PubMed 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 ...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 links | EMBO Rep / PubMed:23877429 / PubMed Central |
Methods | EM (single particle) |
Resolution | 14.5 Å |
Structure data | EMDB-2373: |
Source |
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