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  Structural mechanism of GTPase-powered ribosome-tRNA movement

Petrychenko, V., Peng, B. Z., Schwarzer, A. C. d. A. P., Peske, F., Rodnina, M. V., & Fischer, N. (2021). Structural mechanism of GTPase-powered ribosome-tRNA movement. Nature Communications, 12(1): 5933. doi:10.1038/s41467-021-26133-x.

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 Creators:
Petrychenko, V.1, Author              
Peng, B. Z.2, Author              
Schwarzer, A. C. de A. P., Author
Peske, F.3, Author              
Rodnina, M. V.3, Author              
Fischer, N.1, Author              
Affiliations:
1Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              
2Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578598              
3Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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Free keywords: Cryoelectron microscopy; Ribosome
 Abstract: GTPases are regulators of cell signaling acting as molecular switches. The translational GTPase EF-G stands out, as it uses GTP hydrolysis to generate force and promote the movement of the ribosome along the mRNA. The key unresolved question is how GTP hydrolysis drives molecular movement. Here, we visualize the GTPase-powered step of ongoing translocation by time-resolved cryo-EM. EF-G in the active GDP–Pi form stabilizes the rotated conformation of ribosomal subunits and induces twisting of the sarcin-ricin loop of the 23 S rRNA. Refolding of the GTPase switch regions upon Pi release initiates a large-scale rigid-body rotation of EF-G pivoting around the sarcin-ricin loop that facilitates back rotation of the ribosomal subunits and forward swiveling of the head domain of the small subunit, ultimately driving tRNA forward movement. The findings demonstrate how a GTPase orchestrates spontaneous thermal fluctuations of a large RNA-protein complex into force-generating molecular movement.

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Language(s): eng - English
 Dates: 2021-10-11
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-021-26133-x
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Title: Nature Communications
Source Genre: Journal
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Pages: 9 Volume / Issue: 12 (1) Sequence Number: 5933 Start / End Page: - Identifier: -