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

a 2024

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

HASSAN, Ahmed Adel Ibrahim Hassona, Matyáš PINKAS, Kosuke ITO, Toshio UCHIUMI, Gabriel DEMO et. al.

Základní údaje

Originální název

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

Autoři

HASSAN, Ahmed Adel Ibrahim Hassona (818 Egypt, domácí), Matyáš PINKAS (203 Česká republika, domácí), Kosuke ITO, Toshio UCHIUMI a Gabriel DEMO (703 Slovensko, garant, domácí)

Vydání

RNA society meeting 2024, 2024

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

ribosome subunit dimerization cryoEM structure

Změněno: 12. 9. 2024 10:33, Mgr. Gabriel Demo, Ph.D.

Anotace

V originále

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.

Návaznosti

LL2008, projekt VaV

Název: Komunikace mezi transkripcí a translací (Akronym: CROSSBETT)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Komunikace mezi transkripcí a translací

Citovat

HASSAN, Ahmed Adel Ibrahim Hassona, Matyáš PINKAS, Kosuke ITO, Toshio UCHIUMI a Gabriel DEMO. A novel archaeal ribosome anti-association factor promoting a distinctive 30S-30S dimerization. In RNA society meeting 2024. 2024.

@proceedings{2431822,
   author = {Hassan, Ahmed Adel Ibrahim Hassona and Pinkas, Matyáš and Ito, Kosuke and Uchiumi, Toshio and Demo, Gabriel},
   booktitle = {RNA society meeting 2024},
   keywords = {ribosome subunit dimerization cryoEM structure},
   language = {eng},
   title = {A novel archaeal ribosome anti-association factor promoting a distinctive 30S-30S dimerization},
   url = {https://www2.rnasociety.org/},
   year = {2024}
}

TY  - CONF
ID  - 2431822
AU  - Hassan, Ahmed Adel Ibrahim Hassona - Pinkas, Matyáš - Ito, Kosuke - Uchiumi, Toshio - Demo, Gabriel
PY  - 2024
TI  - A novel archaeal ribosome anti-association factor promoting a distinctive 30S-30S dimerization
KW  - ribosome subunit dimerization cryoEM structure
UR  - https://www2.rnasociety.org/
N2  - 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.
ER  -

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