Structural mechanism of GTPase-powered ribosome-tRNA movement
Structural mechanism of GTPase-powered ribosome-tRNA movement
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 ribosomal subunit rotation and induces twisting of the sarcin-ricin loop of the 23S rRNA. Refolding of the GTPase switch regions upon Pi release initiates a cascade of rearrangements and a large-scale rotation of EF-G that exerts force on the ribosome and ultimately drives tRNA movement. The findings demonstrate how a GTPase orchestrates spontaneous thermal fluctuations of a large RNA-protein complex into force-generating molecular movement.
Fischer Niels、Petrychenko Valentyn、Peske Frank、Peng Bee-Zen、Schwarzer Ana C. de A. P.、Rodnina Marina V.
Department of Structural Dynamics, Max Planck Institute for Biophysical ChemistryDepartment of Structural Dynamics, Max Planck Institute for Biophysical ChemistryDepartment of Physical Biochemistry, Max Planck Institute for Biophysical ChemistryDepartment of Physical Biochemistry, Max Planck Institute for Biophysical ChemistryDepartment of Structural Dynamics, Max Planck Institute for Biophysical ChemistryDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry
生物物理学分子生物学生物化学
Fischer Niels,Petrychenko Valentyn,Peske Frank,Peng Bee-Zen,Schwarzer Ana C. de A. P.,Rodnina Marina V..Structural mechanism of GTPase-powered ribosome-tRNA movement[EB/OL].(2025-03-28)[2025-04-29].https://www.biorxiv.org/content/10.1101/2021.06.01.446629.点此复制
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