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Literature DB >> 23877429

The ribosome triggers the stringent response by RelA via a highly distorted tRNA.

Xabier Agirrezabala¹, Israel S Fernández, Ann C Kelley, David Gil Cartón, Venki Ramakrishnan, Mikel Valle.

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.

Entities: Chemical

Mesh：

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Year: 2013 PMID： 23877429 PMCID： PMC3790049 DOI： 10.1038/embor.2013.106

Source DB: PubMed Journal: EMBO Rep ISSN： 1469-221X Impact factor: 8.807

38 in total

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Review 2. New Insights into Ribosome Structure and Function.

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Review 10. Recent functional insights into the role of (p)ppGpp in bacterial physiology.

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