Crystal structure analysis of the translation factor RF3 (release factor 3)

Kiyohito Kihira, Yoshihiro Shimizu, Yasuhito Shomura, Naoki Shibata, Masaya Kitamura, Atsushi Nakagawa, Takuya Ueda, Kozo Ochi, Yoshiki Higuchi*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)


The bacterial translational GTPases release factor RF3 promotes translation termination by recycling RF1 or RF2. Here, we present the crystal structures of RF3 complexed with GDP and guanosine 3′,5′-(bis)diphosphate (ppGpp) at resolutions of 1.8 and 3.0 Å, respectively. ppGpp is involved in the so-called "stringent response" of bacteria. ppGpp binds at the same site as GDP, suggesting that GDP and ppGpp are two alternative physiologically relevant ligands of RF3. We also found that ppGpp decelerates the recycling of RF1 by RF3. These lines of evidence suggest that RF3 functions both as a cellular metabolic sensor and as a regulator.

Original languageEnglish
Pages (from-to)3705-3709
Number of pages5
JournalFEBS Letters
Issue number20
Publication statusPublished - 2012 Oct 19
Externally publishedYes


  • GTPase
  • Release factor
  • Ribosome
  • Stringent response
  • Translation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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