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Bacteria survival relies on sensing stress. Researchers structurally revealed how RelA enzyme binds stalled ribosomes to trigger the stringent response, a key survival mechanism, offering new antibacterial drug targets.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Structural Biology

Background:

  • Bacteria adapt to environmental changes through stress responses.
  • Stringent control, triggered by nutrient starvation, reprograms bacterial metabolism and gene expression for survival.
  • The alarmone (p)ppGpp, synthesized by RelA, is central to this response.

Purpose of the Study:

  • To elucidate the structural mechanism of RelA binding to stalled bacterial ribosomes.
  • To understand how RelA distinguishes uncharged from aminoacylated tRNAs.
  • To provide a structural basis for targeting RelA in antibacterial drug development.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structure of RelA bound to bacterial ribosomes.
  • Biochemical assays were implied to validate the structural findings.

Main Results:

  • The cryo-EM structure reveals RelA's unique binding site on stalled ribosomes, distinct from other translational factors.
  • RelA's multi-domain architecture interacts with a distorted A-site tRNA.
  • The TGS domain of RelA sterically prevents aminoacylated tRNA binding, facilitating (p)ppGpp synthesis.

Conclusions:

  • The structure explains RelA activation by stalled ribosomes and its discrimination against charged tRNAs.
  • This mechanism initiates the stringent response, crucial for bacterial survival under stress.
  • RelA is a promising target for developing novel therapeutics against pathogenic bacteria.