Unmasking IF2's moves at the start of translation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F25%3A00141989" target="_blank" >RIV/00216224:14740/25:00141989 - isvavai.cz</a>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Unmasking IF2's moves at the start of translation

Popis výsledku v původním jazyce

Bacterial translation initiation is a crucial step in gene expression. It starts with the recruitment of the initiator tRNA to the P-site of the 30S ribosomal subunit, followed by joining of the 50S subunit to form the 70S ribosome. Within the 30S initiation complex (IC), initiation factor 1 (IF1) occupies the A-site, while initiation factor 2 (IF2), a GTPase, promotes subunit joining by facilitating docking of the 50S subunit. This transition to the 70S IC is accompanied by GTP hydrolysis and subsequent dissociation of IF2, ultimately yielding an elongation-competent 70S ribosome. While conformational rearrangements of IF2 have been implicated in its release, the role of its N-terminal domain and the exact timing of IF1 departure remain unclear. Here, we used the α-form of IF2 (E. coli) in combination with time-resolved cryo-EM to address the open questions in bacterial translation initiation. Our results reveal that IF1 dissociates from the 30S subunit prior to 70S IC formation and highlight the stabilizing role of IF2’s N-terminal domain on the 30S subunit during the initiation phase. Additionally, we captured conformational changes in IF2 following GTP hydrolysis, providing a detailed structural view of the molecular events that govern the transition from translation initiation to elongation.

Název v anglickém jazyce

Unmasking IF2's moves at the start of translation

Popis výsledku anglicky

Bacterial translation initiation is a crucial step in gene expression. It starts with the recruitment of the initiator tRNA to the P-site of the 30S ribosomal subunit, followed by joining of the 50S subunit to form the 70S ribosome. Within the 30S initiation complex (IC), initiation factor 1 (IF1) occupies the A-site, while initiation factor 2 (IF2), a GTPase, promotes subunit joining by facilitating docking of the 50S subunit. This transition to the 70S IC is accompanied by GTP hydrolysis and subsequent dissociation of IF2, ultimately yielding an elongation-competent 70S ribosome. While conformational rearrangements of IF2 have been implicated in its release, the role of its N-terminal domain and the exact timing of IF1 departure remain unclear. Here, we used the α-form of IF2 (E. coli) in combination with time-resolved cryo-EM to address the open questions in bacterial translation initiation. Our results reveal that IF1 dissociates from the 30S subunit prior to 70S IC formation and highlight the stabilizing role of IF2’s N-terminal domain on the 30S subunit during the initiation phase. Additionally, we captured conformational changes in IF2 following GTP hydrolysis, providing a detailed structural view of the molecular events that govern the transition from translation initiation to elongation.

Druh

O - Ostatní výsledky

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LX22NPO5103" target="_blank" >LX22NPO5103: Národní institut virologie a bakteriologie</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2025

Kód důvěrnosti údajů

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