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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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
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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. |
format | Online Article Text |
id | pubmed-5737393 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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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