Liquid-liquid phase separation of a bacterial translation factor

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F23%3A00132122" target="_blank" >RIV/00216224:14740/23:00132122 - isvavai.cz</a>

Výsledek na webu

<a href="https://ssbmb2023.sk/" target="_blank" >https://ssbmb2023.sk/</a>

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Liquid-liquid phase separation of a bacterial translation factor

Popis výsledku v původním jazyce

Compartmentalization is a hallmark of living cells that allows them to perform complex tasks by dynamically coordinating matter and energy fluxes in space and time. This compartmentalization of membrane-less organelles in prokaryotes is driven by Liquid-Liquid Phase Separation (LLPS). Studies have shown LLPS to be a major driving force in the subcellular organization of bacterial cells. These biomolecular condensates are comprised of proteins that are generally rich in intrinsically disordered regions (IDRs). In prokaryotes, translation initiation factor 2 (IF-2) is a GTPase that binds the initiator tRNA and catalyses the ribosomal subunit joining to form the elongation competent 70S complex. A large portion of IF-2 contains IDRs, making the protein a favourable candidate for homotypic and/or heterotypic interactions. Here, we present biochemical evidence that IF-2 can phase separate under specific conditions. The IF-2 LLPS formation can provide deeper insight into compartmentalized translation machinery in bacterial cells.

Název v anglickém jazyce

Liquid-liquid phase separation of a bacterial translation factor

Popis výsledku anglicky

Compartmentalization is a hallmark of living cells that allows them to perform complex tasks by dynamically coordinating matter and energy fluxes in space and time. This compartmentalization of membrane-less organelles in prokaryotes is driven by Liquid-Liquid Phase Separation (LLPS). Studies have shown LLPS to be a major driving force in the subcellular organization of bacterial cells. These biomolecular condensates are comprised of proteins that are generally rich in intrinsically disordered regions (IDRs). In prokaryotes, translation initiation factor 2 (IF-2) is a GTPase that binds the initiator tRNA and catalyses the ribosomal subunit joining to form the elongation competent 70S complex. A large portion of IF-2 contains IDRs, making the protein a favourable candidate for homotypic and/or heterotypic interactions. Here, we present biochemical evidence that IF-2 can phase separate under specific conditions. The IF-2 LLPS formation can provide deeper insight into compartmentalized translation machinery in bacterial cells.

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)

Rok uplatnění

2023

Kód důvěrnosti údajů

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