Key result
Topological variations in GTPase factors EF-G, EF4, and BipA determine their diverse roles during translation.
Why the study?
Structural variations among translational GTPase factors EF-G, EF4, and BipA result in different roles during translation that require elucidation from structure to function.
This review highlights the structural basis for the diverse functions of translational GTPase factors EF-G, EF4, and BipA in regulating ribosomal translation.
Does not inform clinical practice; leaves open how EF-G, EF4, and BipA topology might be therapeutically targeted.
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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Ero et al. (2016) reported a review. Translational GTPase factors EF-G, EF4, and BipA was evaluated. Structural studies reveal how topological variations in translational GTPase factors EF-G, EF4, and BipA result in diverse roles and functions during translation.
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