ReviewRNA biology2016
Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function.
Review in RNA biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- An apicoplast-localized GTPase is essential formSphere · 2026Article
- The dual functions of the GTPase BipA in ribosome assembly and surface structure biogenesis in Salmonella enterica serovar Typhimurium.PLoS pathogens · 2025Article
- The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024Review
- Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome.Nucleic acids research · 2023Article
- Novel rRNA transcriptional activity of NhaR revealed by its growth recovery for theFrontiers in molecular biosciences · 2023Article
- Mitogenome-wise codon usage pattern from comparative analysis of the first mitogenome of Blepharipa sp. (Muga uzifly) with other Oestroid flies.Scientific reports · 2022Article
- FERMT1 contributes to the migration and invasion of nasopharyngeal carcinoma through epithelial-mesenchymal transition and cell cycle arrest.Cancer cell international · 2022Article
- Regulation ofFrontiers in microbiology · 2022Review
- Ribosome Protection Proteins-"New" Players in the Global Arms Race with Antibiotic-Resistant Pathogens.International journal of molecular sciences · 2021Review
- Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021Review
- Translational GTPase BipA Is Involved in the Maturation of a Large Subunit of Bacterial Ribosome at Suboptimal Temperature.Frontiers in microbiology · 2021Article
- Elucidation of a Novel Role of YebC in Surface Polysaccharides Regulation ofFrontiers in microbiology · 2020Article
- Overexpressed L20 Rescues 50S Ribosomal Subunit Assembly Defects ofFrontiers in microbiology · 2019Article
- The GTPase BipA expressed at low temperature inThe Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
EF-G, EF4, and BipA are members of the translation factor family of GTPases with a common ribosome binding mode and GTPase activation mechanism. However, topological variations of shared as well as unique domains ensure different roles played by these proteins during translation. Recent X-ray crystallography and cryo-electron microscopy studies have revealed the structural basis for the involvement of EF-G domain IV in securing the movement of tRNAs and mRNA during translocation as well as revealing how the unique C-terminal domains of EF4 and BipA interact with the ribosome and tRNAs contributing to the regulation of translation under certain conditions. EF-G, EF-4, and BipA are intriguing examples of structural variations on a common theme that results in diverse behavior and function. Structural studies of translational GTPase factors have been greatly facilitated by the use of antibiotics, which have revealed their mechanism of action.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.