Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function. Issue 12 (1st December 2016)

• Record Type: Journal Article
• Authors: Ero, Rya; Kumar, Veerendra; Chen, Yun; Gao, Yong-Gui
• Is Part Of: RNA biology. Volume 13:Issue 12(2016)
• Page Start: 1258
• Page End: 1273
• Publication Date: 2016-12-01
• Subjects: BipA -- EF-G -- EF4 -- ribosome -- translocation -- trGTPase; RNA -- Periodicals; Molecular biology -- Periodicals; Molecular biology; RNA; Periodicals; 572.8805
• DOI: 10.1080/15476286.2016.1201627
• Languages: English
• ISSNs: 1547-6286

Abstract

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.