A novel archaeal ribosome anti-association factor promoting a distinctive  30S-30S dimerization

Warning

This publication doesn't include Faculty of Sports Studies. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.

Authors	HASSAN Ahmed Adel Ibrahim Hassona PINKAS Matyáš ITO Kosuke UCHIUMI Toshio DEMO Gabriel
Year of publication	2024
Type	Conference abstract
MU Faculty or unit	Central European Institute of Technology
Citation
Description	Protein synthesis consumes a substantial portion of cellular resources, prompting specialized mechanisms to reduce the translation during adverse conditions. Ribosome inactivation often involves ribosome-interacting proteins. During stationary phase, ribosome modulation factor (RMF) and hibernation-promoting factor (HPF) in some ?-proteobacteria initiate the formation of translationally inactive 100S ribosome dimers. Additionally, bacteria utilize ribosome silencing or anti-association factors to prevent active 70S ribosome formation. Despite extensive studies in bacteria, insights into factor-mediated ribosome dimerization or anti-association in archaea remain elusive. Here, we present the first cryo-electron microscopy structures of archaeal 30S dimer complexed with a novel archaeal ribosome dimerization factor (termed as aRDF) from Pyrococcus furiosus. The complex exhibits two 30S subunits stabilized by aRDF homodimers in a head-to-body architecture. aRDF interacts directly with the L41e ribosomal protein, essential for subunit association. The binding mode of aRDF demonstrates its anti-association ability, preventing the assembly of archaeal 70S ribosomes.
Related projects:	Crosstalk between transcription and translation