Structural insights into ribosome anti-association mechanism in archaea

Kód výsledku v 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>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Structural insights into ribosome anti-association mechanism in archaea

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Structural insights into ribosome anti-association mechanism in archaea

Popis výsledku anglicky

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.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LX22NPO5103" target="_blank" >LX22NPO5103: Národní institut virologie a bakteriologie</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2025

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů