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Length-dependent translation efficiency of ER-destined proteins

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00843989%3A_____%2F23%3AE0110364" target="_blank" >RIV/00843989:_____/23:E0110364 - isvavai.cz</a>

  • Alternative codes found

    RIV/61988987:17110/23:A2402N76

  • Result on the web

    <a href="https://www.mdpi.com/1467-3045/45/8/425" target="_blank" >https://www.mdpi.com/1467-3045/45/8/425</a>

  • DOI - Digital Object Identifier

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

Alternative languages

  • Result language

    angličtina

  • Original language name

    Length-dependent translation efficiency of ER-destined proteins

  • Original language description

    Gene expression is a fundamental process that enables cells to produce specific proteins in a timely and spatially dependent manner. In eukaryotic cells, the complex organization of the cell body requires precise control of protein synthesis and localization. Certain mRNAs encode proteins with an N-terminal signal sequences that direct the translation apparatus toward a specific organelle. Here, we focus on the mechanisms governing the translation of mRNAs, which encode proteins with an endoplasmic reticulum (ER) signal in human cells. The binding of a signal-recognition particle (SRP) to the translation machinery halts protein synthesis until the mRNA-ribosome complex reaches the ER membrane. The commonly accepted model suggests that mRNA that encodes a protein that contains an ER signal peptide continuously repeats the cycle of SRP binding followed by association and dissociation with the ER. In contrast to the current view, we show that the long mRNAs remain on the ER while being translated. On the other hand, due to low ribosome occupancy, the short mRNAs continue the cycle, always facing a 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

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10601 - Cell biology

Result continuities

  • 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)

Others

  • Publication year

    2023

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Current issues in molecular biology

  • ISSN

    1467-3037

  • e-ISSN

    1467-3045

  • Volume of the periodical

    45

  • 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