Intrinsic molecular properties of the protein-protein bridge facilitate ratchet-like motion of the ribosome

Biochemical and Biophysical Research Communications
Manidip ShasmalJayati Sengupta

Abstract

The ribosomal intersubunit bridges maintain the overall architecture of the ribosome and thereby play a pivotal role in the dynamics of translation. The only protein-protein bridge, b1b, is formed by the two proteins, S13 and L5 of the small and large ribosomal subunits, respectively. B1b absorbs the largest movement during ratchet-like motion, and its two proteins reorganize in different constellations during this motion of the ribosome. Our results in this study of b1b in the Escherichia coli 70S ribosome suggest that the intrinsic molecular features of the bridging proteins allow the bridge to modulate the ratchet-like motion in a controlled manner. Additionally, another large subunit protein, L31, seems to participate with S13 and L5 in the formation, dynamics, and stabilization of this bridge.

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Citations

Aug 22, 2012·Current Opinion in Structural Biology·Joachim Frank
Feb 18, 2016·Journal of Molecular Biology·Qi Liu, Kurt Fredrick
Feb 1, 2017·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Joachim Frank
Jun 20, 2020·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Masami UetaAkira Wada
Dec 18, 2020·International Journal of Molecular Sciences·Sokuntheary ThengMichael J Franklin

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