Publication details
INVOLVEMENT OF A NOVEL RIBOSOME ASSOCIATED FACTOR INTRANSLATION REGULATION
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| Year of publication | 2024 |
| Type | Appeared in Conference without Proceedings |
| MU Faculty or unit | |
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| Description | Ribosome inactivation is a vital adaptive mechanism that allows the cells to conserve resources under stress by controlling protein synthesis1–3. Although ribosome-interacting proteins in facilitating ribosome dimerization and hibernation are well studied in bacteria and eukaryotes4–8, similar mechanisms in archaea remain poorly understood. Here we present high-resolution cryo-electron microscopy structures of an archaeal 30S ribosomal dimer stabilized by a ribosome dimerization factor (aRDF) from Pyrococcus furiosus. Structures were resolved at 3.2 A with a unique head-to-body architecture of the 30S ribosomal subunits, distinct from the dimerized ribosome structures observed in other domains of life. The aRDF protein interacts directly with the eS32 ribosomal protein, a key player in subunit association. Therefore, based on biochemical and structural evidence aRDF ´s function is to halt the assembly of functional 70S ribosomes. These findings provide novel insights into ribosome inactivation mechanisms in archaea presenting aRDF as an archaeal ribosome anti-association factor that inhibits ribosome subunit joining for translational control purposes (Scheme 1). |
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