Cryo-EM ensemble captures EF-G mediated ribosomal translocation in action

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F21%3A00122989" target="_blank" >RIV/00216224:14740/21:00122989 - isvavai.cz</a>

Výsledek na webu

<a href="https://csbmb2021.cz/detailed-programme/" target="_blank" >https://csbmb2021.cz/detailed-programme/</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Cryo-EM ensemble captures EF-G mediated ribosomal translocation in action

Popis výsledku v původním jazyce

During protein synthesis, transfer RNAs (tRNAs) and messenger RNA (mRNA) codons are translocated within the ribosome from the A to P to E sites, respectively. Translocation of tRNAs anticodons and mRNA along the small ribosomal 30S subunit is catalyzed by a conserved GTPase, elongation factor G(EF-G) in bacteria. The structural mechanism how the ribosome and EF-G maintain the open reading frame has not been visualized because the rapid GTP hydrolysis step has prevented the capture of authentic EF-G bound structural intermediates. Here, we present our single particle cryo-EM study aimed at characterizing translocation without using EF-G mutations or antibiotics. We report newly described intermediate structural state, which visualized the transition of two tRNAs from the A and P to P and E sites during translocation. The structure visualizes how nearly rigid EF-G rectifies inherent and spontaneous ribosomal dynamics into tRNA and mRNA translocation. This work therefore uncovers a missing link in the understanding of the synchronous movement of tRNAs and mRNA during translation elongation.

Název v anglickém jazyce

Cryo-EM ensemble captures EF-G mediated ribosomal translocation in action

Popis výsledku anglicky

During protein synthesis, transfer RNAs (tRNAs) and messenger RNA (mRNA) codons are translocated within the ribosome from the A to P to E sites, respectively. Translocation of tRNAs anticodons and mRNA along the small ribosomal 30S subunit is catalyzed by a conserved GTPase, elongation factor G(EF-G) in bacteria. The structural mechanism how the ribosome and EF-G maintain the open reading frame has not been visualized because the rapid GTP hydrolysis step has prevented the capture of authentic EF-G bound structural intermediates. Here, we present our single particle cryo-EM study aimed at characterizing translocation without using EF-G mutations or antibiotics. We report newly described intermediate structural state, which visualized the transition of two tRNAs from the A and P to P and E sites during translocation. The structure visualizes how nearly rigid EF-G rectifies inherent and spontaneous ribosomal dynamics into tRNA and mRNA translocation. This work therefore uncovers a missing link in the understanding of the synchronous movement of tRNAs and mRNA during translation elongation.

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

2021

Kód důvěrnosti údajů

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