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Converting GTP hydrolysis into motion: versatile translational elongation factor G

Authors
  • Rodnina, Marina V.1
  • Peske, Frank1
  • Peng, Bee-Zen1
  • Belardinelli, Riccardo1
  • Wintermeyer, Wolfgang1
  • 1 Max Planck Institute for Biophysical Chemistry, Am Fassberg 11 , (Germany)
Type
Published Article
Journal
Biological Chemistry
Publisher
Walter de Gruyter GmbH
Publication Date
Oct 09, 2019
Volume
401
Issue
1
Pages
131–142
Identifiers
DOI: 10.1515/hsz-2019-0313
Source
De Gruyter
Keywords
License
Yellow

Abstract

Elongation factor G (EF-G) is a translational GTPase that acts at several stages of protein synthesis. Its canonical function is to catalyze tRNA movement during translation elongation, but it also acts at the last step of translation to promote ribosome recycling. Moreover, EF-G has additional functions, such as helping the ribosome to maintain the mRNA reading frame or to slide over non-coding stretches of the mRNA. EF-G has an unconventional GTPase cycle that couples the energy of GTP hydrolysis to movement. EF-G facilitates movement in the GDP-Pi form. To convert the energy of hydrolysis to movement, it requires various ligands in the A site, such as a tRNA in translocation, an mRNA secondary structure element in ribosome sliding, or ribosome recycling factor in post-termination complex disassembly. The ligand defines the direction and timing of EF-G-facilitated motion. In this review, we summarize recent advances in understanding the mechanism of EF-G action as a remarkable force-generating GTPase.

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