Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon
Regulation of protein synthesis contributes to maintenance of homeostasis and adaptation to environmental changes. mRNA translation is controlled at various levels including initiation, elongation and termination, through post-transcriptional/translational modifications of components of the protein...
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1420682X_v73_n9_p1881_Katz http://hdl.handle.net/20.500.12110/paper_1420682X_v73_n9_p1881_Katz |
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paper:paper_1420682X_v73_n9_p1881_Katz2023-06-08T16:13:46Z Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon Wappner, Pablo Dioxygenases Post-translational modifications Protein synthesis Translational fidelity elongation factor ribosome protein transfer RNA dioxygenase ribosome protein stop codon transfer RNA cell stress codon human hydroxylation nonhuman protein synthesis Review stop codon stop codon read through transcription elongation transcription termination translation regulation bacterium genetics hydroxylation metabolism oxidative stress protein processing stop codon Bacteria Codon, Terminator Dioxygenases Humans Hydroxylation Oxidative Stress Protein Processing, Post-Translational Ribosomal Proteins RNA, Transfer Regulation of protein synthesis contributes to maintenance of homeostasis and adaptation to environmental changes. mRNA translation is controlled at various levels including initiation, elongation and termination, through post-transcriptional/translational modifications of components of the protein synthesis machinery. Recently, protein and RNA hydroxylation have emerged as important enzymatic modifications of tRNAs, elongation and termination factors, as well as ribosomal proteins. These modifications enable a correct STOP codon recognition, ensuring translational fidelity. Recent studies are starting to show that STOP codon read-through is related to the ability of the cell to cope with different types of stress, such as oxidative and chemical insults, while correlations between defects in hydroxylation of protein synthesis components and STOP codon read-through are beginning to emerge. In this review we will discuss our current knowledge of protein synthesis regulation through hydroxylation of components of the translation machinery, with special focus on STOP codon recognition. We speculate on the possibility that programmed STOP codon read-through, modulated by hydroxylation of components of the protein synthesis machinery, is part of a concerted cellular response to stress. © 2016 Springer International Publishing. Fil:Wappner, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2016 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1420682X_v73_n9_p1881_Katz http://hdl.handle.net/20.500.12110/paper_1420682X_v73_n9_p1881_Katz |
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Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Dioxygenases Post-translational modifications Protein synthesis Translational fidelity elongation factor ribosome protein transfer RNA dioxygenase ribosome protein stop codon transfer RNA cell stress codon human hydroxylation nonhuman protein synthesis Review stop codon stop codon read through transcription elongation transcription termination translation regulation bacterium genetics hydroxylation metabolism oxidative stress protein processing stop codon Bacteria Codon, Terminator Dioxygenases Humans Hydroxylation Oxidative Stress Protein Processing, Post-Translational Ribosomal Proteins RNA, Transfer |
| spellingShingle |
Dioxygenases Post-translational modifications Protein synthesis Translational fidelity elongation factor ribosome protein transfer RNA dioxygenase ribosome protein stop codon transfer RNA cell stress codon human hydroxylation nonhuman protein synthesis Review stop codon stop codon read through transcription elongation transcription termination translation regulation bacterium genetics hydroxylation metabolism oxidative stress protein processing stop codon Bacteria Codon, Terminator Dioxygenases Humans Hydroxylation Oxidative Stress Protein Processing, Post-Translational Ribosomal Proteins RNA, Transfer Wappner, Pablo Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon |
| topic_facet |
Dioxygenases Post-translational modifications Protein synthesis Translational fidelity elongation factor ribosome protein transfer RNA dioxygenase ribosome protein stop codon transfer RNA cell stress codon human hydroxylation nonhuman protein synthesis Review stop codon stop codon read through transcription elongation transcription termination translation regulation bacterium genetics hydroxylation metabolism oxidative stress protein processing stop codon Bacteria Codon, Terminator Dioxygenases Humans Hydroxylation Oxidative Stress Protein Processing, Post-Translational Ribosomal Proteins RNA, Transfer |
| description |
Regulation of protein synthesis contributes to maintenance of homeostasis and adaptation to environmental changes. mRNA translation is controlled at various levels including initiation, elongation and termination, through post-transcriptional/translational modifications of components of the protein synthesis machinery. Recently, protein and RNA hydroxylation have emerged as important enzymatic modifications of tRNAs, elongation and termination factors, as well as ribosomal proteins. These modifications enable a correct STOP codon recognition, ensuring translational fidelity. Recent studies are starting to show that STOP codon read-through is related to the ability of the cell to cope with different types of stress, such as oxidative and chemical insults, while correlations between defects in hydroxylation of protein synthesis components and STOP codon read-through are beginning to emerge. In this review we will discuss our current knowledge of protein synthesis regulation through hydroxylation of components of the translation machinery, with special focus on STOP codon recognition. We speculate on the possibility that programmed STOP codon read-through, modulated by hydroxylation of components of the protein synthesis machinery, is part of a concerted cellular response to stress. © 2016 Springer International Publishing. |
| author |
Wappner, Pablo |
| author_facet |
Wappner, Pablo |
| author_sort |
Wappner, Pablo |
| title |
Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon |
| title_short |
Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon |
| title_full |
Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon |
| title_fullStr |
Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon |
| title_full_unstemmed |
Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon |
| title_sort |
hydroxylation and translational adaptation to stress: some answers lie beyond the stop codon |
| publishDate |
2016 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1420682X_v73_n9_p1881_Katz http://hdl.handle.net/20.500.12110/paper_1420682X_v73_n9_p1881_Katz |
| work_keys_str_mv |
AT wappnerpablo hydroxylationandtranslationaladaptationtostresssomeanswersliebeyondthestopcodon |
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1768544195374481408 |