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Unanchored ubiquitin chains do not lead to marked alterations in gene expression in Drosophila melanogaster
The small protein modifier ubiquitin regulates various aspects of cellular biology through its chemical conjugation onto proteins. Ubiquitination of proteins presents itself in numerous iterations, from a single mono-ubiquitination event to chains of poly-ubiquitin. Ubiquitin chains can be attached...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists Ltd
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6550069/ https://www.ncbi.nlm.nih.gov/pubmed/31097444 http://dx.doi.org/10.1242/bio.043372 |
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author | Blount, Jessica R. Meyer, Danielle N. Akemann, Camille Johnson, Sean L. Gurdziel, Katherine Baker, Tracie R. Todi, Sokol V. |
author_facet | Blount, Jessica R. Meyer, Danielle N. Akemann, Camille Johnson, Sean L. Gurdziel, Katherine Baker, Tracie R. Todi, Sokol V. |
author_sort | Blount, Jessica R. |
collection | PubMed |
description | The small protein modifier ubiquitin regulates various aspects of cellular biology through its chemical conjugation onto proteins. Ubiquitination of proteins presents itself in numerous iterations, from a single mono-ubiquitination event to chains of poly-ubiquitin. Ubiquitin chains can be attached onto other proteins or can exist as unanchored species, i.e. free from another protein. Unanchored ubiquitin chains are thought to be deleterious to the cell and rapidly disassembled into mono-ubiquitin. We recently examined the toxicity and utilization of unanchored poly-ubiquitin in Drosophila melanogaster. We found that free poly-ubiquitin species are largely innocuous to flies and that free poly-ubiquitin can be controlled by being degraded by the proteasome or by being conjugated onto another protein as a single unit. Here, to explore whether an organismal defense is mounted against unanchored chains, we conducted RNA-Seq analyses to examine the transcriptomic impact of free poly-ubiquitin in the fly. We found ∼90 transcripts whose expression is altered in the presence of different types of unanchored poly-ubiquitin. The set of genes identified was essentially devoid of ubiquitin-, proteasome-, or autophagy-related components. The seeming absence of a large and multipronged response to unanchored poly-ubiquitin supports the conclusion that these species need not be toxic in vivo and underscores the need to re-examine the role of free ubiquitin chains in the cell. |
format | Online Article Text |
id | pubmed-6550069 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The Company of Biologists Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-65500692019-06-07 Unanchored ubiquitin chains do not lead to marked alterations in gene expression in Drosophila melanogaster Blount, Jessica R. Meyer, Danielle N. Akemann, Camille Johnson, Sean L. Gurdziel, Katherine Baker, Tracie R. Todi, Sokol V. Biol Open Research Article The small protein modifier ubiquitin regulates various aspects of cellular biology through its chemical conjugation onto proteins. Ubiquitination of proteins presents itself in numerous iterations, from a single mono-ubiquitination event to chains of poly-ubiquitin. Ubiquitin chains can be attached onto other proteins or can exist as unanchored species, i.e. free from another protein. Unanchored ubiquitin chains are thought to be deleterious to the cell and rapidly disassembled into mono-ubiquitin. We recently examined the toxicity and utilization of unanchored poly-ubiquitin in Drosophila melanogaster. We found that free poly-ubiquitin species are largely innocuous to flies and that free poly-ubiquitin can be controlled by being degraded by the proteasome or by being conjugated onto another protein as a single unit. Here, to explore whether an organismal defense is mounted against unanchored chains, we conducted RNA-Seq analyses to examine the transcriptomic impact of free poly-ubiquitin in the fly. We found ∼90 transcripts whose expression is altered in the presence of different types of unanchored poly-ubiquitin. The set of genes identified was essentially devoid of ubiquitin-, proteasome-, or autophagy-related components. The seeming absence of a large and multipronged response to unanchored poly-ubiquitin supports the conclusion that these species need not be toxic in vivo and underscores the need to re-examine the role of free ubiquitin chains in the cell. The Company of Biologists Ltd 2019-05-16 /pmc/articles/PMC6550069/ /pubmed/31097444 http://dx.doi.org/10.1242/bio.043372 Text en © 2019. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/4.0This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
spellingShingle | Research Article Blount, Jessica R. Meyer, Danielle N. Akemann, Camille Johnson, Sean L. Gurdziel, Katherine Baker, Tracie R. Todi, Sokol V. Unanchored ubiquitin chains do not lead to marked alterations in gene expression in Drosophila melanogaster |
title | Unanchored ubiquitin chains do not lead to marked alterations in gene expression in Drosophila melanogaster |
title_full | Unanchored ubiquitin chains do not lead to marked alterations in gene expression in Drosophila melanogaster |
title_fullStr | Unanchored ubiquitin chains do not lead to marked alterations in gene expression in Drosophila melanogaster |
title_full_unstemmed | Unanchored ubiquitin chains do not lead to marked alterations in gene expression in Drosophila melanogaster |
title_short | Unanchored ubiquitin chains do not lead to marked alterations in gene expression in Drosophila melanogaster |
title_sort | unanchored ubiquitin chains do not lead to marked alterations in gene expression in drosophila melanogaster |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6550069/ https://www.ncbi.nlm.nih.gov/pubmed/31097444 http://dx.doi.org/10.1242/bio.043372 |
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