Length-dependent translation efficiency of ER-destined proteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61988987%3A17110%2F23%3AA2502K31" target="_blank" >RIV/61988987:17110/23:A2502K31 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61988987:17110/23:A2402N76 RIV/00843989:_____/23:E0110364

Výsledek na webu

<a href="https://www.biorxiv.org/content/10.1101/2023.03.16.532890v1.full" target="_blank" >https://www.biorxiv.org/content/10.1101/2023.03.16.532890v1.full</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/cimb45080425" target="_blank" >10.3390/cimb45080425</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Length-dependent translation efficiency of ER-destined proteins

Popis výsledku v původním jazyce

Gene expression resulting in the generation of new proteins is a fundamental process critical for every living organism. Particularly in eukaryotic cells, complex organization of the cell body requires fine-tuning of every step prior to de novo protein synthesis. To ensure proper localization, certain mRNAs possess unique signal sequence, which destinies the translation apparatus to the specific organelle. Here we focus on the mechanisms governing the translation of signal sequence-bearing mRNAs, which encode proteins targeted to the endoplasmic reticulum (ER). The binding of a signal-recognition particle (SRP) to the translation machinery halts protein synthesis until the mRNA-ribosome complex reaches ER membrane. The commonly accepted model suggests that mRNA containing the ER signal peptide continuously repeats the cycle of SRP binding followed by association and dissociation with ER. In contrast with the current view, we show that the long mRNAs remain on the ER while being translated. On the other hand, due to a low ribosome occupancy, the short mRNAs continue the cycle always facing the translation pause. Ultimately, this leads to a significant drop in the translation efficiency of small, ER-targeted proteins. The proposed mechanism advances our understanding of selective protein synthesis in eukaryotic cells and provides new avenues to enhance protein production in biotechnological settings.

Název v anglickém jazyce

Length-dependent translation efficiency of ER-destined proteins

Popis výsledku anglicky

Gene expression resulting in the generation of new proteins is a fundamental process critical for every living organism. Particularly in eukaryotic cells, complex organization of the cell body requires fine-tuning of every step prior to de novo protein synthesis. To ensure proper localization, certain mRNAs possess unique signal sequence, which destinies the translation apparatus to the specific organelle. Here we focus on the mechanisms governing the translation of signal sequence-bearing mRNAs, which encode proteins targeted to the endoplasmic reticulum (ER). The binding of a signal-recognition particle (SRP) to the translation machinery halts protein synthesis until the mRNA-ribosome complex reaches ER membrane. The commonly accepted model suggests that mRNA containing the ER signal peptide continuously repeats the cycle of SRP binding followed by association and dissociation with ER. In contrast with the current view, we show that the long mRNAs remain on the ER while being translated. On the other hand, due to a low ribosome occupancy, the short mRNAs continue the cycle always facing the translation pause. Ultimately, this leads to a significant drop in the translation efficiency of small, ER-targeted proteins. The proposed mechanism advances our understanding of selective protein synthesis in eukaryotic cells and provides new avenues to enhance protein production in biotechnological settings.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10601 - Cell biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

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

Název periodika

CURR ISSUES MOL BIOL

ISSN

1467-3037

e-ISSN

1467-3045

Svazek periodika

—

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

11

Strana od-do

6717-6727

Kód UT WoS článku

001119117800001

EID výsledku v databázi Scopus

2-s2.0-85169039218