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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 bacteria 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. The binding mode of aRDF demonstrates its anti-association ability, preventing the assembly of archaeal 70S ribosomes.
