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Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
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The ribosome termination complex remodels release factor RF3 and ejects GDP.

Li Li1,2, Mariia Yu Rybak3, Jinzhong Lin4,5

  • 1State Key Laboratory of Genetic Engineering, School of Life Sciences, Zhongshan Hospital, Fudan University, Shanghai, China.

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|July 19, 2024
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The 70S ribosome termination complex (70S-TC) acts as a guanine nucleotide exchange factor, facilitating GDP release from release factor 3 (RF3). This ribosome remodeling mechanism ensures efficient recycling of release factors during translation termination.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Translation termination relies on release factors (RF1, RF2) and the GTPase RF3 for recycling.
  • RF3 must exchange GDP for GTP after dissociating from the ribosome to re-enter the cycle.
  • The 70S ribosome termination complex (70S-TC) is known to accelerate this GDP/GTP exchange for RF3.

Purpose of the Study:

  • To elucidate the mechanism of GDP dissociation from RF3 catalyzed by the Escherichia coli 70S-TC.
  • To understand the structural basis of RF3 recycling during translation termination.

Main Methods:

  • Cryogenic-electron microscopy (cryo-EM) was used to determine high-resolution structures.
  • Structural analysis of the 70S-TC bound to RF1 and RF3.

Main Results:

  • The non-rotated ribosome bound to RF1 remodels RF3, inducing a peptide flip that ejects GDP.
  • GTP binding enables RF3 to dock at the GTPase center, promoting RF1 dissociation.
  • The 70S-TC allosterically dismantles the phosphate-binding groove in RF3, facilitating GDP release.

Conclusions:

  • The 70S-TC functions as a guanine nucleotide exchange factor for RF3.
  • Structural insights reveal a novel ribosome-mediated mechanism for RF3 GDP/GTP exchange.
  • This study uncovers a previously unrecognized allosteric function of the ribosome in regulating release factor recycling.