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Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle

Protein synthesis is mediated via numerous molecules including the ribosome, mRNA, tRNAs, as well as translation initiation, elongation and release factors. Some of these factors play several roles throughout the entire process to ensure proper assembly of the preinitiation complex on the right mRNA...

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Autores principales: Valášek, Leoš Shivaya, Zeman, Jakub, Wagner, Susan, Beznosková, Petra, Pavlíková, Zuzana, Mohammad, Mahabub Pasha, Hronová, Vladislava, Herrmannová, Anna, Hashem, Yaser, Gunišová, Stanislava
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5737393/
https://www.ncbi.nlm.nih.gov/pubmed/28981723
http://dx.doi.org/10.1093/nar/gkx805
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author Valášek, Leoš Shivaya
Zeman, Jakub
Wagner, Susan
Beznosková, Petra
Pavlíková, Zuzana
Mohammad, Mahabub Pasha
Hronová, Vladislava
Herrmannová, Anna
Hashem, Yaser
Gunišová, Stanislava
author_facet Valášek, Leoš Shivaya
Zeman, Jakub
Wagner, Susan
Beznosková, Petra
Pavlíková, Zuzana
Mohammad, Mahabub Pasha
Hronová, Vladislava
Herrmannová, Anna
Hashem, Yaser
Gunišová, Stanislava
author_sort Valášek, Leoš Shivaya
collection PubMed
description Protein synthesis is mediated via numerous molecules including the ribosome, mRNA, tRNAs, as well as translation initiation, elongation and release factors. Some of these factors play several roles throughout the entire process to ensure proper assembly of the preinitiation complex on the right mRNA, accurate selection of the initiation codon, errorless production of the encoded polypeptide and its proper termination. Perhaps, the most intriguing of these multitasking factors is the eukaryotic initiation factor eIF3. Recent evidence strongly suggests that this factor, which coordinates the progress of most of the initiation steps, does not come off the initiation complex upon subunit joining, but instead it remains bound to 80S ribosomes and gradually falls off during the first few elongation cycles to: (1) promote resumption of scanning on the same mRNA molecule for reinitiation downstream—in case of translation of upstream ORFs short enough to preserve eIF3 bound; or (2) come back during termination on long ORFs to fine tune its fidelity or, if signaled, promote programmed stop codon readthrough. Here, we unite recent structural views of the eIF3–40S complex and discus all known eIF3 roles to provide a broad picture of the eIF3’s impact on translational control in eukaryotic cells.
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spelling pubmed-57373932018-01-08 Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle Valášek, Leoš Shivaya Zeman, Jakub Wagner, Susan Beznosková, Petra Pavlíková, Zuzana Mohammad, Mahabub Pasha Hronová, Vladislava Herrmannová, Anna Hashem, Yaser Gunišová, Stanislava Nucleic Acids Res Survey and Summary Protein synthesis is mediated via numerous molecules including the ribosome, mRNA, tRNAs, as well as translation initiation, elongation and release factors. Some of these factors play several roles throughout the entire process to ensure proper assembly of the preinitiation complex on the right mRNA, accurate selection of the initiation codon, errorless production of the encoded polypeptide and its proper termination. Perhaps, the most intriguing of these multitasking factors is the eukaryotic initiation factor eIF3. Recent evidence strongly suggests that this factor, which coordinates the progress of most of the initiation steps, does not come off the initiation complex upon subunit joining, but instead it remains bound to 80S ribosomes and gradually falls off during the first few elongation cycles to: (1) promote resumption of scanning on the same mRNA molecule for reinitiation downstream—in case of translation of upstream ORFs short enough to preserve eIF3 bound; or (2) come back during termination on long ORFs to fine tune its fidelity or, if signaled, promote programmed stop codon readthrough. Here, we unite recent structural views of the eIF3–40S complex and discus all known eIF3 roles to provide a broad picture of the eIF3’s impact on translational control in eukaryotic cells. Oxford University Press 2017-11-02 2017-09-14 /pmc/articles/PMC5737393/ /pubmed/28981723 http://dx.doi.org/10.1093/nar/gkx805 Text en © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Survey and Summary
Valášek, Leoš Shivaya
Zeman, Jakub
Wagner, Susan
Beznosková, Petra
Pavlíková, Zuzana
Mohammad, Mahabub Pasha
Hronová, Vladislava
Herrmannová, Anna
Hashem, Yaser
Gunišová, Stanislava
Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle
title Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle
title_full Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle
title_fullStr Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle
title_full_unstemmed Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle
title_short Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle
title_sort embraced by eif3: structural and functional insights into the roles of eif3 across the translation cycle
topic Survey and Summary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5737393/
https://www.ncbi.nlm.nih.gov/pubmed/28981723
http://dx.doi.org/10.1093/nar/gkx805
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