Distinct 30S subunit dimerization architecture facilitated by a
novel ribosome dimerization factor in archaea

a 2024

Distinct 30S subunit dimerization architecture facilitated by a novel ribosome dimerization factor in archaea

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

Základní údaje

Originální název

Distinct 30S subunit dimerization architecture facilitated by a novel ribosome dimerization factor in archaea

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

XX Discussions in Structural Molecular Biology, 2024

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Organizační jednotka

Středoevropský technologický institut

ISSN

Klíčová slova anglicky

ribosome subunit dimerization cryoEM structure

Štítky

NIVB_CEITEC, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 12. 9. 2024 16:14, Mgr. Eva Dubská

Anotace

V originále

Protein synthesis utilizes a significant portion of the cell's available resources. In the face of unfavourable conditions, specialized mechanisms come into play to reduce the overall costly protein synthesis. Several ribosome-associated factors play a role in this regulation in bacteria. Some induce an inactive, hibernating state in the ribosome, forming 70S monomers (such as RaiA) or 100S dimers (RMF and HPF). Other factors hinder translation at various stages in the translation cycle acting as anti-association factors not allowing the formation of 70S ribosome (such as RsfS). Therefore, ribosome dimerization and anti-association are important regulatory events to inactivate the protein synthesis in bacteria and enable their survival under various stress conditions. While the hibernation and anti-association mechanisms have been extensively studied in various bacterial species, the ribosomal response to adverse conditions causing growth arrest is not well understood in archaea and eukaryotes. Here, we describe the first single particle cryo-electron microscopy structures of archaeal 30S dimers bound to a novel archaeal ribosome dimerization factor (aRDF)6. The overall arrangement of the 30S-30S dimer exhibits a head-to-body orientation connected by two homodimers of aRDF. aRDF forms a direct interaction with the L41e ribosomal protein, a key player in the establishment of a ribosomal bridge during subunit association. Therefore, the binding mode of aRDF illustrates its anti-association capability, preventing the formation of archaeal 70S ribosomes. Thus, the comprehensive structural architecture of aRDF-mediated 30S subunit dimerization provides unprecedented insights into the mechanism of ribosome shutdown in archaea.

Návaznosti

LX22NPO5103, projekt VaV

Název: Národní institut virologie a bakteriologie (Akronym: NIVB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Národní institut virologie a bakteriologie, 5.1 EXCELES

Citovat

HASSAN, Ahmed Adel Ibrahim Hassona, Matyáš PINKAS, Kosuke ITO, Toshio UCHIUMI a Gabriel DEMO. Distinct 30S subunit dimerization architecture facilitated by a novel ribosome dimerization factor in archaea. In XX Discussions in Structural Molecular Biology. 2024. ISSN 1805-4382.

@proceedings{2431799,
   author = {Hassan, Ahmed Adel Ibrahim Hassona and Pinkas, Matyáš and Ito, Kosuke and Uchiumi, Toshio and Demo, Gabriel},
   booktitle = {XX Discussions in Structural Molecular Biology},
   keywords = {ribosome subunit dimerization cryoEM structure},
   language = {eng},
   title = {Distinct 30S subunit dimerization architecture facilitated by a novel ribosome dimerization factor in archaea},
   url = {https://cssb.structbio.org/xx-discussions-in-structural-molecular-biology-and-7th-user-meeting-of-ciisb-czech-infrastructure-for-integrative-structural-biologyp/},
   year = {2024}
}

TY  - CONF
ID  - 2431799
AU  - Hassan, Ahmed Adel Ibrahim Hassona - Pinkas, Matyáš - Ito, Kosuke - Uchiumi, Toshio - Demo, Gabriel
PY  - 2024
TI  - Distinct 30S subunit dimerization architecture facilitated by a novel ribosome dimerization factor in archaea
KW  - ribosome subunit dimerization cryoEM structure
UR  - https://cssb.structbio.org/xx-discussions-in-structural-molecular-biology-and-7th-user-meeting-of-ciisb-czech-infrastructure-for-integrative-structural-biologyp/
N2  - Protein synthesis utilizes a significant portion of the cell's available resources. In the face of unfavourable conditions, specialized mechanisms come into play to reduce the overall costly protein synthesis. Several ribosome-associated factors play a role in this regulation in bacteria. Some induce an inactive, hibernating state in the ribosome, forming 70S monomers (such as RaiA) or 100S dimers (RMF and HPF). Other factors hinder translation at various stages in the translation cycle acting as anti-association factors not allowing the formation of 70S ribosome (such as RsfS). Therefore, ribosome dimerization and anti-association are important regulatory events to inactivate the protein synthesis in bacteria and enable their survival under various stress conditions. While the hibernation and anti-association mechanisms have been extensively studied in various bacterial species, the ribosomal response to adverse conditions causing growth arrest is not well understood in archaea and eukaryotes. Here, we describe the first single particle cryo-electron microscopy structures of archaeal 30S dimers bound to a novel archaeal ribosome dimerization factor (aRDF)6. The overall arrangement of the 30S-30S dimer exhibits a head-to-body orientation connected by two homodimers of aRDF. aRDF forms a direct interaction with the L41e ribosomal protein, a key player in the establishment of a ribosomal bridge during subunit association. Therefore, the binding mode of aRDF illustrates its anti-association capability, preventing the formation of archaeal 70S ribosomes. Thus, the comprehensive structural architecture of aRDF-mediated 30S subunit dimerization provides unprecedented insights into the mechanism of ribosome shutdown in archaea.
ER  -

HASSAN, Ahmed Adel Ibrahim Hassona, Matyáš PINKAS, Kosuke ITO, Toshio UCHIUMI a Gabriel DEMO. Distinct 30S subunit dimerization architecture facilitated by a novel ribosome dimerization factor in archaea. In \textit{XX Discussions in Structural Molecular Biology}. 2024. ISSN~1805-4382.

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