Unusual Antioxidant Properties of 26S Proteasome Isolated from Cold-Adapted Organisms
The oxidative challenge represents an important factor affecting the adaptive strategies in Antarctic fish, but their impact on the protein degradation machinery still remains unclear. The previous analysis of the first 26S proteasome from the Antarctic red-blooded fish Trematomus bernacchii, eviden...
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ftpubmed:oai:pubmedcentral.nih.gov:5577997 2023-05-15T13:53:52+02:00 Unusual Antioxidant Properties of 26S Proteasome Isolated from Cold-Adapted Organisms Gogliettino, Marta Cocca, Ennio Fusco, Carmela Agrillo, Bruna Riccio, Alessia Balestrieri, Marco Facchiano, Angelo Pepe, Antonio Palmieri, Gianna 2017-07-25 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5577997/ http://www.ncbi.nlm.nih.gov/pubmed/28757562 https://doi.org/10.3390/ijms18081605 en eng MDPI http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5577997/ http://www.ncbi.nlm.nih.gov/pubmed/28757562 http://dx.doi.org/10.3390/ijms18081605 © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). CC-BY Article Text 2017 ftpubmed https://doi.org/10.3390/ijms18081605 2017-09-10T00:08:35Z The oxidative challenge represents an important factor affecting the adaptive strategies in Antarctic fish, but their impact on the protein degradation machinery still remains unclear. The previous analysis of the first 26S proteasome from the Antarctic red-blooded fish Trematomus bernacchii, evidenced improved antioxidant functions necessary to counteract the environmental pro-oxidant conditions. The purpose of this work was to carry out a study on 26S proteasomes from the temperate red-blooded Dicenthrarcus labrax and the icefish Chionodraco hamatus in comparison with the isoform already described from T. bernacchii, to better elucidate the cold-adapted physiological functions of this complex. Therefore, the 26S isoforms were isolated and the complementary DNAs (cDNAs) codifying the catalytic subunits were cloned. The biochemical characterization of Antarctic 26S proteasomes revealed their significantly higher structural stability and resistance to H2O2 with respect to that of the temperate counterpart, as also suggested by a comparative modeling analysis of the catalytic subunits. Moreover, in contrast to that observed in T. bernacchii, the 26S systems from C. hamatus and D. labrax were incapable to hydrolyze oxidized proteins in a ubiquitin-independent manner. Therefore, the ‘uncommon’ properties displayed by the Antarctic 26S proteasomes can mirror the impact exercised by evolutionary pressure in response to richly oxygenated environments. Text Antarc* Antarctic Icefish PubMed Central (PMC) Antarctic The Antarctic International Journal of Molecular Sciences 18 8 1605 |
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Article Gogliettino, Marta Cocca, Ennio Fusco, Carmela Agrillo, Bruna Riccio, Alessia Balestrieri, Marco Facchiano, Angelo Pepe, Antonio Palmieri, Gianna Unusual Antioxidant Properties of 26S Proteasome Isolated from Cold-Adapted Organisms |
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The oxidative challenge represents an important factor affecting the adaptive strategies in Antarctic fish, but their impact on the protein degradation machinery still remains unclear. The previous analysis of the first 26S proteasome from the Antarctic red-blooded fish Trematomus bernacchii, evidenced improved antioxidant functions necessary to counteract the environmental pro-oxidant conditions. The purpose of this work was to carry out a study on 26S proteasomes from the temperate red-blooded Dicenthrarcus labrax and the icefish Chionodraco hamatus in comparison with the isoform already described from T. bernacchii, to better elucidate the cold-adapted physiological functions of this complex. Therefore, the 26S isoforms were isolated and the complementary DNAs (cDNAs) codifying the catalytic subunits were cloned. The biochemical characterization of Antarctic 26S proteasomes revealed their significantly higher structural stability and resistance to H2O2 with respect to that of the temperate counterpart, as also suggested by a comparative modeling analysis of the catalytic subunits. Moreover, in contrast to that observed in T. bernacchii, the 26S systems from C. hamatus and D. labrax were incapable to hydrolyze oxidized proteins in a ubiquitin-independent manner. Therefore, the ‘uncommon’ properties displayed by the Antarctic 26S proteasomes can mirror the impact exercised by evolutionary pressure in response to richly oxygenated environments. |
format |
Text |
author |
Gogliettino, Marta Cocca, Ennio Fusco, Carmela Agrillo, Bruna Riccio, Alessia Balestrieri, Marco Facchiano, Angelo Pepe, Antonio Palmieri, Gianna |
author_facet |
Gogliettino, Marta Cocca, Ennio Fusco, Carmela Agrillo, Bruna Riccio, Alessia Balestrieri, Marco Facchiano, Angelo Pepe, Antonio Palmieri, Gianna |
author_sort |
Gogliettino, Marta |
title |
Unusual Antioxidant Properties of 26S Proteasome Isolated from Cold-Adapted Organisms |
title_short |
Unusual Antioxidant Properties of 26S Proteasome Isolated from Cold-Adapted Organisms |
title_full |
Unusual Antioxidant Properties of 26S Proteasome Isolated from Cold-Adapted Organisms |
title_fullStr |
Unusual Antioxidant Properties of 26S Proteasome Isolated from Cold-Adapted Organisms |
title_full_unstemmed |
Unusual Antioxidant Properties of 26S Proteasome Isolated from Cold-Adapted Organisms |
title_sort |
unusual antioxidant properties of 26s proteasome isolated from cold-adapted organisms |
publisher |
MDPI |
publishDate |
2017 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5577997/ http://www.ncbi.nlm.nih.gov/pubmed/28757562 https://doi.org/10.3390/ijms18081605 |
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Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
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Antarc* Antarctic Icefish |
genre_facet |
Antarc* Antarctic Icefish |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5577997/ http://www.ncbi.nlm.nih.gov/pubmed/28757562 http://dx.doi.org/10.3390/ijms18081605 |
op_rights |
© 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
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CC-BY |
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https://doi.org/10.3390/ijms18081605 |
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International Journal of Molecular Sciences |
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18 |
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1605 |
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