Conformational changes associated with ribosome function have been identified by X-ray crystallography and cryo-electron microscopy. These methods, however, inform poorly on timescales. Neutron scattering is well adapted for direct measurements of thermal molecular dynamics, the 'lubricant' for the conformational fluctuations required for biological activity. The method was applied to compare water dynamics and conformational fluctuations in the 30 S and 50 S ribosomal subunits from Haloarcula marismortui, under high salt, stable conditions. Similar free and hydration water diffusion parameters are found for both subunits. With respect to the 50 S subunit, the 30 S is characterized by a softer force constant and larger mean square displacements (MSD), which would facilitate conformational adjustments required for messenger and transfer RNA binding. It has been shown previously that systems from mesophiles and extremophiles are adapted to have similar MSD under their respective physiological conditions. This suggests that the results presented are not specific to halophiles in high salt but a general property of ribosome dynamics under corresponding, active conditions. The current study opens new perspectives for neutron scattering characterization of component functional molecular dynamics within the ribosome.

CNR IOM OGG F 38042 Grenoble France

Institut Charles Sadron CNRS UdS 67034 Strasbourg Cedex 2 France

Institut de Biologie Structurale Univ Grenoble Alpes CEA CNRS 38044 Grenoble France

Institut de Systématique Evolution Biodiversité ISYEB UMR 7205 CNRS MNHN UPMC EPHE UPMC Sorbonne Universités 57 rue Cuvier CP 50 75005 Paris France

Institut Laue Langevin F 38042 Grenoble France

Institute of Physics Charles University Faculty of Mathematics and Physics CZ 121 16 Prague Czech Republic

Univ Grenoble Alpes LiPhy F 38044 Grenoble France

Weizmann Institute Department of Structural Biology 76100 Rehovot Israel

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