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

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.

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 Creators:
Rodnina, M. V.1, Author           
Peske, F.1, Author           
Peng, B. Z.1, Author           
Belardinelli, R.1, Author           
Wintermeyer, W.2, Author           
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1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              
2Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578599              

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Free keywords: protein synthesis; reading frame maintenance; ribosome bypassing; ribosome recycling; translocation
 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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Language(s): eng - English
 Dates: 2019-10-302019-12-18
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1515/hsz-2019-0313
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Title: Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 401 (1) Sequence Number: - Start / End Page: 131 - 142 Identifier: -