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The ribosome triggers the stringent response by RelA via a highly distorted tRNA
Author(s) -
Agirrezabala Xabier,
Fernández Israel S,
Kelley Ann C,
Cartón David Gil,
Ramakrishnan Venki,
Valle Mikel
Publication year - 2013
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2013.106
Subject(s) - ribosome , stringent response , transfer rna , t arm , biology , ef tu , protein biosynthesis , gene , biochemistry , genetics , chemistry , microbiology and biotechnology , rna , escherichia coli
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.