A novel archaeal ribosome anti-association factor promoting a distinctive 30S-30S dimerization

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F24%3A00137094" target="_blank" >RIV/00216224:14740/24:00137094 - 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

A novel archaeal ribosome anti-association factor promoting a distinctive 30S-30S dimerization

Popis výsledku v původním jazyce

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 γ-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.

Název v anglickém jazyce

A novel archaeal ribosome anti-association factor promoting a distinctive 30S-30S dimerization

Popis výsledku anglicky

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 γ-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.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LL2008" target="_blank" >LL2008: Komunikace mezi transkripcí a translací</a><br>

Návaznosti

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

Rok uplatnění

2024

Kód důvěrnosti údajů

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