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Cloning and expression analysis of Drosophila extracellular Cu Zn superoxide dismutase
In the present study, we cloned and sequenced the mRNAs of the Sod3 [extracellular Cu Zn SOD (superoxide dismutase)] gene in Drosophila and identified two mRNA products formed by alternative splicing. These products code for a long and short protein derived from the four transcripts found in global...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4274663/ https://www.ncbi.nlm.nih.gov/pubmed/25339624 http://dx.doi.org/10.1042/BSR20140133 |
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author | Blackney, Michael J. Cox, Rebecca Shepherd, David Parker, Joel D. |
author_facet | Blackney, Michael J. Cox, Rebecca Shepherd, David Parker, Joel D. |
author_sort | Blackney, Michael J. |
collection | PubMed |
description | In the present study, we cloned and sequenced the mRNAs of the Sod3 [extracellular Cu Zn SOD (superoxide dismutase)] gene in Drosophila and identified two mRNA products formed by alternative splicing. These products code for a long and short protein derived from the four transcripts found in global expression studies (Flybase numbers Dmel\CG9027, FBgn0033631). Both mRNA process variants contain an extracellular signalling sequence, a region of high homology to the Sod1 (cytoplasmic Cu Zn SOD) including a conserved AUG start, with the longer form also containing a hydrophobic tail. The two fully processed transcripts are homologous to Caenorhabditis elegans Sod3 mRNA showing the same processing pattern. Using an established KG p-element+ insertion line (KG06029), we demonstrate that the Sod3 codes for an active Cu Zn SOD. We found differing expression patterns across sex with higher levels of expression of Sod3 in females. There is a correlation of Sod1 and Sod3 gene expression and activity that can explain why Sod3 was not seen in earlier studies of Sod1. Finally, we found no effect on lifespan with the Sod3 hypomorph mutation (Sod3(KG06029)) but did observe a significant increase in resistance to paraquat and H(2)O(2) (hydrogen peroxide). |
format | Online Article Text |
id | pubmed-4274663 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-42746632014-12-30 Cloning and expression analysis of Drosophila extracellular Cu Zn superoxide dismutase Blackney, Michael J. Cox, Rebecca Shepherd, David Parker, Joel D. Biosci Rep Original Paper In the present study, we cloned and sequenced the mRNAs of the Sod3 [extracellular Cu Zn SOD (superoxide dismutase)] gene in Drosophila and identified two mRNA products formed by alternative splicing. These products code for a long and short protein derived from the four transcripts found in global expression studies (Flybase numbers Dmel\CG9027, FBgn0033631). Both mRNA process variants contain an extracellular signalling sequence, a region of high homology to the Sod1 (cytoplasmic Cu Zn SOD) including a conserved AUG start, with the longer form also containing a hydrophobic tail. The two fully processed transcripts are homologous to Caenorhabditis elegans Sod3 mRNA showing the same processing pattern. Using an established KG p-element+ insertion line (KG06029), we demonstrate that the Sod3 codes for an active Cu Zn SOD. We found differing expression patterns across sex with higher levels of expression of Sod3 in females. There is a correlation of Sod1 and Sod3 gene expression and activity that can explain why Sod3 was not seen in earlier studies of Sod1. Finally, we found no effect on lifespan with the Sod3 hypomorph mutation (Sod3(KG06029)) but did observe a significant increase in resistance to paraquat and H(2)O(2) (hydrogen peroxide). Portland Press Ltd. 2014-12-23 /pmc/articles/PMC4274663/ /pubmed/25339624 http://dx.doi.org/10.1042/BSR20140133 Text en © 2014 The Author(s) This is an Open Access article distributed under the terms of the Creative Commons Attribution Licence (CC-BY) (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Licence (CC-BY) (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Paper Blackney, Michael J. Cox, Rebecca Shepherd, David Parker, Joel D. Cloning and expression analysis of Drosophila extracellular Cu Zn superoxide dismutase |
title | Cloning and expression analysis of Drosophila extracellular Cu Zn superoxide dismutase |
title_full | Cloning and expression analysis of Drosophila extracellular Cu Zn superoxide dismutase |
title_fullStr | Cloning and expression analysis of Drosophila extracellular Cu Zn superoxide dismutase |
title_full_unstemmed | Cloning and expression analysis of Drosophila extracellular Cu Zn superoxide dismutase |
title_short | Cloning and expression analysis of Drosophila extracellular Cu Zn superoxide dismutase |
title_sort | cloning and expression analysis of drosophila extracellular cu zn superoxide dismutase |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4274663/ https://www.ncbi.nlm.nih.gov/pubmed/25339624 http://dx.doi.org/10.1042/BSR20140133 |
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