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.

Basic information

Original name

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

Authors

HASSAN, Ahmed Adel Ibrahim Hassona (818 Egypt, belonging to the institution), Matyáš PINKAS (203 Czech Republic, belonging to the institution), Kosuke ITO, Toshio UCHIUMI and Gabriel DEMO (703 Slovakia, guarantor, belonging to the institution)

Edition

XX Discussions in Structural Molecular Biology, 2024

Other information

Language

English

Type of outcome

Konferenční abstrakt

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Czech Republic

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Organization unit

Central European Institute of Technology

ISSN

Keywords in English

ribosome subunit dimerization cryoEM structure

Abstract

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.

Links

LX22NPO5103, research and development project

Name: Národní institut virologie a bakteriologie (Acronym: NIVB)

Investor: Ministry of Education, Youth and Sports of the CR, National Institute of Virology and Bacteriology, 5.1 EXCELES

Citovat

HASSAN, Ahmed Adel Ibrahim Hassona, Matyáš PINKAS, Kosuke ITO, Toshio UCHIUMI and 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 and 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.

Detailed Information on Publication Record