HASSAN, Ahmed Adel I. H., Kosuke ITO, Toshio UCHIUMI and Gabriel DEMO. Ribosome hibernation in archaea. In XXVIIth Biochemistry congress of Czech Society for Biochemistry and Molecular Biology. 2023. ISBN 978-80-8240-047-5.
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Basic information
Original name Ribosome hibernation in archaea
Name in Czech Hibernace ribozomů u archaei
Authors HASSAN, Ahmed Adel I. H., Kosuke ITO, Toshio UCHIUMI and Gabriel DEMO.
Edition XXVIIth Biochemistry congress of Czech Society for Biochemistry and Molecular Biology, 2023.
Other information
Original language English
Type of outcome Konferenční abstrakta
Country of publisher Slovakia
Confidentiality degree is not subject to a state or trade secret
WWW URL
Organization Středoevropský technologický institut – Repository – Repository
ISBN 978-80-8240-047-5
Keywords (in Czech) ribozom; dimerizační faktor; kryoEM; struktura
Keywords in English ribosome; dimerization factor; cryoEM; structure
Links LX22NPO5103, research and development project.
Changed by Changed by: RNDr. Daniel Jakubík, učo 139797. Changed: 11/11/2023 03:13.
Abstract
Under stress conditions in bacterial cells, the formation of a hibernating ribosome dimer (termed 100S), is a useful adaptation mechanism, which results in suppression of protein synthesis in the stationary phase. In E. coli, two protein factors, RMF and HPF, are involved in regulation of dimerization of the 70S ribosome. RMF directly participates in dimerization of 70S ribosomes and HPF stabilizes the 100S ribosomes. However, homologous proteins of RMF and HPF have not been found in archaea. Therefore, further investigations of the molecular mechanisms of ribosome hibernation in archaea are required. Here, we present a single particle cryo-EM study, revealing a novel ribosome dimerization factor (RDF) in archea. The RDF is highly specific to archeal ribosomes and is capable to interact only with archeal 30S small ribosomal subunit. In order to determine the structure of the novel RDF new approaches of de novo model building were used in combination with artificial intelligence (AI). The overall architecture of the 30S-30S dimer shows a head to body orientation. The RDF links the head and body regions of two distinct 30S molecules in the form of a dimer. The binding position of the RDF monomeric structure on the head of 30S subunit implies a mechanistic role to regulate the mRNA binding on the 30S subunit. In turn, the 30S subunits are unable to initiate the translation and stay in a hibernation mode.
Abstract (in Czech)
Za stresových podmínek v bakteriálních buňkách je tvorba hibernujícího ribozomového dimeru (označovaného jako 100S) užitečným adaptačním mechanismem, jehož výsledkem je potlačení syntézy proteinů ve stacionární fázi. U E. coli se na regulaci dimerizace ribozomu 70S podílejí dva proteinové faktory, RMF a HPF. RMF se přímo podílí na dimerizaci 70S ribozomů a HPF stabilizuje 100S ribozomy. Nicméně homologní proteiny RMF a HPF nebyly nalezeny v archaei. Proto jsou zapotřebí výzkum molekulárních mechanismů hibernace ribozomů u archaei. Zde uvádíme studii kryo-EM, která odhaluje nový faktor dimerizace ribozomů (RDF) v archei. RDF je vysoce specifický pro archeální ribozomy a je schopen interagovat pouze s archeální 30S malou ribozomální podjednotkou. Aby bylo možné určit strukturu nového RDF, byly použity nové přístupy k budování de novo modelu v kombinaci s umělou inteligencí (AI). Celková architektura dimeru 30S-30S ukazuje orientaci hlavy na tělo. RDF spojuje oblasti hlavy a těla dvou odlišných molekul 30S ve formě dimeru. Vazebná poloha RDF monomerní struktury na hlavě podjednotky 30S implikuje mechanickou roli při regulaci vazby mRNA na podjednotku 30S. Na druhé straně podjednotky 30S nejsou schopny zahájit translaci a zůstavaji v režimu hibernace.
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  • a concrete person Mgr. Lucie Vařechová, uco 106253
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  • a concrete person Mgr. Jolana Surýnková, uco 220973
  • a concrete person Mgr. Michal Maňas, uco 2481
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