Structural insights into ribosome anti-association mechanism in archaea

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F25%3A00141640" target="_blank" >RIV/00216224:14740/25:00141640 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Structural insights into ribosome anti-association mechanism in archaea
Original language description
Protein synthesis (translation) consumes a significant portion of cellular resources, necessitating specialized mechanisms to modulate translation during adverse conditions. Ribosome inactivation often involves ribosome-interacting proteins that enable ribosome dimerization, hibernation, or subunit anti-association, allowing organisms to adapt to stress. While such mechanisms are well-characterized in bacteria and eukaryotes, factor-mediated ribosome dimerization or anti-association in archaea has remained largely unexplored. Here, we present cryo-electron microscopy (cryo-EM) structures of an archaeal 30S dimer complexed with an archaeal ribosome dimerization factor (aRDF) from Pyrococcus furiosus. The aRDF-stabilized 30S dimer adopts a unique head-to-body architecture, distinct from the disome conformation observed during bacterial1,2 and eukaryotic ribosome hibernation4. aRDF interacts directly with the eS32 ribosomal protein, a critical component for subunit association, revealing its anti-association properties that inhibit the formation of archaeal 70S ribosomes. The archaeal system employs a unique strategy, offering valuable insights into ribosome inactivation and uncovering distinct mechanisms of ribosomal regulation across domains of life.
Czech name
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Czech description
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Project
<a href="/en/project/LX22NPO5103" target="_blank" >LX22NPO5103: National Institute of Virology and Bacteriology</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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