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Converting GTP hydrolysis into motion: Versatile translational elongation factor G.

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Rodnina,  M. V.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Peske,  F.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Peng,  B. Z.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Belardinelli,  R.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Wintermeyer,  W.
Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Rodnina, M. V., Peske, F., Peng, B. Z., Belardinelli, R., & Wintermeyer, W. (2019). Converting GTP hydrolysis into motion: Versatile translational elongation factor G. Biological Chemistry, 401(1), 131-142. doi:10.1515/hsz-2019-0313.


Cite as: http://hdl.handle.net/21.11116/0000-0005-0A4C-C
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.