ArticleThe Biochemical journal2006
Domain II plays a crucial role in the function of ribosome recycling factor.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Mechanistic insights into the alternative ribosome recycling by HflXr.Nucleic acids research · 2024Article
- Mechanisms of ribosome recycling in bacteria and mitochondria: a structural perspective.RNA biology · 2022Review
- Structural basis for ribosome recycling by RRF and tRNA.Nature structural & molecular biology · 2020Article
- Structural insights into unique features of the human mitochondrial ribosome recycling.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Purification, crystallization and preliminary crystallographic analysis of a ribosome-recycling factor from Thermoanaerobacter tengcongensis (TteRRF).Acta crystallographica. Section F, Structural biology communications · 2014Article
- A dual sensor for real-time monitoring of glucose and oxygen.Biomaterials · 2013Article
- Structural insights into initial and intermediate steps of the ribosome-recycling process.The EMBO journal · 2012Article
- Structural Insights into ribosome recycling factor interactions with the 70S ribosome.Journal of molecular biology · 2008Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 TteRRF, 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 concerted 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.
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