Length-dependent translation efficiency of ER-destined proteins

Result code in 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>

Alternative codes found

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

Result on the web

<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>

Result language

angličtina

Original language name

Length-dependent translation efficiency of ER-destined proteins

Original language description

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.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10601 - Cell biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2023

Confidentiality

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

Name of the periodical

CURR ISSUES MOL BIOL

ISSN

1467-3037

e-ISSN

1467-3045

Volume of the periodical

—

Issue of the periodical within the volume

8

Country of publishing house

CH - SWITZERLAND

Number of pages

11

Pages from-to

6717-6727

UT code for WoS article

001119117800001

EID of the result in the Scopus database

2-s2.0-85169039218