ArticleThe EMBO journal2001
Specific interaction between the ribosome recycling factor and the elongation factor G from Mycobacterium tuberculosis mediates peptidyl-tRNA release and ribosome recycling in Escherichia coli.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 89 citations in OpenAlex.
- Functional loss ofFrontiers in microbiology · 2025Article
- Quality control of protein synthesis in the early elongation stage.Nature communications · 2023Article
- Peptidyl tRNA Hydrolase Is Required for Robust Prolyl-tRNA Turnover in Mycobacterium tuberculosis.mBio · 2023Article
- Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance.Nature communications · 2021Article
- Label-Free Comparative Proteomics of Differentially ExpressedPathogens (Basel, Switzerland) · 2021Article
- Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021Review
- Mitochondrial Protein Translation: Emerging Roles and Clinical Significance in Disease.Frontiers in cell and developmental biology · 2021Review
- 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
- Species-Specific Interactions of Arr with RplK Mediate Stringent Response in Bacteria.Journal of bacteriology · 2018Article
- Advances inSynthetic biology (Oxford, England) · 2018Article
- tRNA engineering for manipulating genetic code.RNA biology · 2018Review
- A Possible Role of the Full-Length Nascent Protein in Post-Translational Ribosome Recycling.PloS one · 2017Article
- HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions.Nature structural & molecular biology · 2015Article
- Fusidic acid targets elongation factor G in several stages of translocation on the bacterial ribosome.The Journal of biological chemistry · 2015Article
- Purification, crystallization and preliminary crystallographic analysis of a ribosome-recycling factor from Thermoanaerobacter tengcongensis (TteRRF).Acta crystallographica. Section F, Structural biology communications · 2014Article
- Molecular flexibility of Mycobacterium tuberculosis ribosome recycling factor and its functional consequences: an exploration involving mutants.Journal of biosciences · 2013Article
- Initiation with elongator tRNAs.Journal of bacteriology · 2013Article
- Mycobacterium tuberculosis MutT1 (Rv2985) and ADPRase (Rv1700) proteins constitute a two-stage mechanism of 8-oxo-dGTP and 8-oxo-GTP detoxification and adenosine to cytidine mutation avoidance.The Journal of biological chemistry · 2013Article
- Identical RNA-protein interactions in vivo and in vitro and a scheme of folding the newly synthesized proteins by ribosomes.The Journal of biological chemistry · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Once the translating ribosomes reach a termination codon, the nascent polypeptide chain is released in a factor-dependent manner. However, the P-site-bound deacylated tRNA and the ribosomes themselves remain bound to the mRNA (post-termination complex). The ribosome recycling factor (RRF) plays a vital role in dissociating this complex. Here we show that the Mycobacterium tuberculosis RRF (MtuRRF) fails to rescue Escherichia coli LJ14, a strain temperature-sensitive for RRF (frr(ts)). More interestingly, co-expression of M.tuberculosis elongation factor G (MtuEFG) with MtuRRF rescues the frr(ts) strain of E.coli. The simultaneous expression of MtuEFG is also needed to cause an enhanced release of peptidyl-tRNAs in E.coli by MtuRRF. These observations provide the first genetic evidence for a functional interaction between RRF and EFG. Both the in vivo and in vitro analyses suggest that RRF does not distinguish between the translating and terminating ribosomes for their dissociation from mRNA. In addition, complementation of E.coli PEM100 (fusA(ts)) with MtuEFG suggests that the mechanism of RRF function is independent of the translocation activity of EFG.
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