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The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its cellular localization and stress response
Transient modification of the environment involves the expression of specific genes and degradation of mRNAs and proteins. How these events are linked is poorly understood. CCR4-NOT is an evolutionary conserved complex involved in transcription initiation and mRNA degradation. In this paper, we repo...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8370887/ https://www.ncbi.nlm.nih.gov/pubmed/34338747 http://dx.doi.org/10.1093/femsle/fnab097 |
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author | Palermo, Vanessa Stirpe, Mariarita Bianchi, Michele Maria Rinaldi, Teresa Cirigliano, Angela Ragnini-Wilson, Antonella Falcone, Claudio Mazzoni, Cristina |
author_facet | Palermo, Vanessa Stirpe, Mariarita Bianchi, Michele Maria Rinaldi, Teresa Cirigliano, Angela Ragnini-Wilson, Antonella Falcone, Claudio Mazzoni, Cristina |
author_sort | Palermo, Vanessa |
collection | PubMed |
description | Transient modification of the environment involves the expression of specific genes and degradation of mRNAs and proteins. How these events are linked is poorly understood. CCR4-NOT is an evolutionary conserved complex involved in transcription initiation and mRNA degradation. In this paper, we report that the yeast Not4 localizes in cytoplasmic foci after cellular stress. We focused our attention on the functional characterization of the C-terminus of the Not4 protein. Molecular dissection of this region indicates that the removal of the last 120 amino acids, does not affect protein localization and function, in that the protein is still able to suppress the thermosensitivity observed in the not4Δ mutant. In addition, such shortened form of Not4, as well its absence, increases the transcription of stress-responsive genes conferring to the cell high resistance to the oxidative stress. On the contrary, the last C-terminal 211 amino acids are required for proper Not4 localization at cytoplasmic foci after stress. This truncated version of Not4 fails to increase the transcription of the stress genes, is more stable and seems to be toxic to cells undergoing oxidative stress. |
format | Online Article Text |
id | pubmed-8370887 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-83708872021-08-18 The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its cellular localization and stress response Palermo, Vanessa Stirpe, Mariarita Bianchi, Michele Maria Rinaldi, Teresa Cirigliano, Angela Ragnini-Wilson, Antonella Falcone, Claudio Mazzoni, Cristina FEMS Microbiol Lett Research Letter Transient modification of the environment involves the expression of specific genes and degradation of mRNAs and proteins. How these events are linked is poorly understood. CCR4-NOT is an evolutionary conserved complex involved in transcription initiation and mRNA degradation. In this paper, we report that the yeast Not4 localizes in cytoplasmic foci after cellular stress. We focused our attention on the functional characterization of the C-terminus of the Not4 protein. Molecular dissection of this region indicates that the removal of the last 120 amino acids, does not affect protein localization and function, in that the protein is still able to suppress the thermosensitivity observed in the not4Δ mutant. In addition, such shortened form of Not4, as well its absence, increases the transcription of stress-responsive genes conferring to the cell high resistance to the oxidative stress. On the contrary, the last C-terminal 211 amino acids are required for proper Not4 localization at cytoplasmic foci after stress. This truncated version of Not4 fails to increase the transcription of the stress genes, is more stable and seems to be toxic to cells undergoing oxidative stress. Oxford University Press 2021-08-02 /pmc/articles/PMC8370887/ /pubmed/34338747 http://dx.doi.org/10.1093/femsle/fnab097 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of FEMS. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial-NoDerivs licence (https://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Research Letter Palermo, Vanessa Stirpe, Mariarita Bianchi, Michele Maria Rinaldi, Teresa Cirigliano, Angela Ragnini-Wilson, Antonella Falcone, Claudio Mazzoni, Cristina The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its cellular localization and stress response |
title | The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its
cellular localization and stress response |
title_full | The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its
cellular localization and stress response |
title_fullStr | The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its
cellular localization and stress response |
title_full_unstemmed | The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its
cellular localization and stress response |
title_short | The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its
cellular localization and stress response |
title_sort | c-terminal region of yeast ubiquitin–protein ligase not4 mediates its
cellular localization and stress response |
topic | Research Letter |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8370887/ https://www.ncbi.nlm.nih.gov/pubmed/34338747 http://dx.doi.org/10.1093/femsle/fnab097 |
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