Domain II plays a crucial role in the function of ribosome recycling factor

Peng Guo, Liqiang Zhang, Hongjie Zhang, Vanning Feng, Guozhong Jing

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


RRF (ribosome recycling factor) consists of two domains, and in concert with EF-G (elongation factor-G), triggers dissociation of the post-termination ribosomal complex. However, the function of the individual domains of RRF remains unclear. To clarify this, two RRF chimaeras, EcoDI/TteDII and TteDI/EcoDII, were created by domain swaps between the proteins from Escherichia coli and Thermoanaerobacter tengcongensis. The ribosome recycling activity of the RRF chimaeras was compared with their wild-type RRFs by using in vivo and in vitro activity assays. Like wild-type TteRRF (T. tengcongensis RRF), the EcoDI/TteDII chimaera is non-functional in E. coli, but both wild-type TYeRRF, and EcoDI/TteDII can be activated by coexpression of T. tengcongensis EF-G in E. coli. By contrast, like wild-type E. coli RRF (EcoRRF), TteDI/EcoDII is fully functional in E. coli. These findings suggest that domain II of RRF plays a crucial role in the conceited action of RRF and EF-G for the post-termination complex disassembly, and the specific interaction between RRF and EF-G on ribosomes mainly depends on the interaction between domain II of RRF and EF-G. This study provides direct genetic and biochemical evidence for the function of the individual domains of RRF.

Original languageEnglish (US)
Pages (from-to)767-777
Number of pages11
JournalBiochemical Journal
Issue number3
StatePublished - Feb 1 2006
Externally publishedYes


  • Domain function
  • Domain swaps
  • Elongation factor (EF-G)
  • Escherichia coli
  • Ribosome recycling factor (RRF)
  • Thermoanaerobacter tengcongensis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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