Publication details
A novel archaeal ribosome anti-association factor promoting a distinctive 30S-30S dimerization
| Authors | |
|---|---|
| Year of publication | 2024 |
| Type | Conference abstract |
| MU Faculty or unit | |
| 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: |