Dissection of the mechanism for the stringent factor RelA.

  title={Dissection of the mechanism for the stringent factor RelA.},
  author={Thomas M Wendrich and Gregor M. Blaha and Daniel N. Wilson and Mohamed A. Marahiel and Knud H. Nierhaus},
  journal={Molecular cell},
  volume={10 4},
During conditions of nutrient deprivation, ribosomes are blocked by uncharged tRNA at the A site. The stringent factor RelA binds to blocked ribosomes and catalyzes synthesis of (p)ppGpp, a secondary messenger that induces the stringent response. We demonstrate that binding of RelA and (p)ppGpp synthesis are inversely coupled, i.e., (p)ppGpp synthesis decreases the affinity of RelA for the ribosome. RelA binding to ribosomes is governed primarily by mRNA, but independently of ribosomal protein… CONTINUE READING

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Publications referenced by this paper.
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Ribosomes and polysomes

D. Richter
View 6 Excerpts
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Dimerization of the RelA protein of Escherichia coli.

Biochemistry and cell biology = Biochimie et biologie cellulaire • 2001
View 2 Excerpts
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Threestringent factor

N. Burkhardt, R. Jünemann, C. M. T. Spahn, F. J. Alonso, K. H. Nierhaus
J . Biol . Chem . • 1996

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