Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii
Protein homoeostasis is a fundamental process allowing the preservation of functional proteins and it has a great impact on the life of the Antarctic organisms. However, the effect of low temperatures on protein turnover is poorly understood and the cold-adaptation of the degradation machinery remai...
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Online Access: | http://dx.doi.org/10.1042/bsr20160022 https://portlandpress.com/bioscirep/article-pdf/doi/10.1042/BSR20160022/477677/bsr036e320.pdf |
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crportlandpress:10.1042/bsr20160022 2024-09-15T17:43:09+00:00 Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii Gogliettino, Marta Balestrieri, Marco Riccio, Alessia Facchiano, Angelo Fusco, Carmela Palazzo, Vincenzo Cecere Rossi, Mosè Cocca, Ennio Palmieri, Gianna 2016 http://dx.doi.org/10.1042/bsr20160022 https://portlandpress.com/bioscirep/article-pdf/doi/10.1042/BSR20160022/477677/bsr036e320.pdf en eng Portland Press Ltd. http://creativecommons.org/licenses/by/4.0/ Bioscience Reports volume 36, issue 2 ISSN 0144-8463 1573-4935 journal-article 2016 crportlandpress https://doi.org/10.1042/bsr20160022 2024-07-11T04:20:09Z Protein homoeostasis is a fundamental process allowing the preservation of functional proteins and it has a great impact on the life of the Antarctic organisms. However, the effect of low temperatures on protein turnover is poorly understood and the cold-adaptation of the degradation machinery remains an unresolved issue. As the 26S proteasome represents the main proteolytic system devoted to the controlled degradation of intracellular proteins, the purpose of the present study was to investigate the functions of this complex in the notothenioid Trematomus bernacchii, in order to better understand its role in the physiology of Antarctic fish. To this aim, we purified and characterized the 26S proteasome from T. bernacchii and isolated the cDNAs codifying seven of the 14 subunits belonging to the proteasome 20S core particle. Results provided evidences of the high resistance of the piscine 26S proteasome to oxidative agents and of its ‘uncommon’ ability to efficiently hydrolyse oxidized bovine serum albumin (BSA), suggesting that this enzymatic complex could play a key role in the antioxidant defense systems in fish inhabiting permanently cold marine environments. These unique properties were also reflected by the 3D model analysis, which revealed a higher structural stability of the piscine complex respect to the murine template. Finally, a comparative analysis, performed in a variety of tissues collected from T. bernacchii and the temperate fish Dicentrarchus labrax, showed a lower protein retention in the cold-adapted fish, possibly due to a better efficiency of its degradation machinery. Article in Journal/Newspaper Antarc* Antarctic Portland Press Bioscience Reports 36 2 |
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Portland Press |
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English |
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Protein homoeostasis is a fundamental process allowing the preservation of functional proteins and it has a great impact on the life of the Antarctic organisms. However, the effect of low temperatures on protein turnover is poorly understood and the cold-adaptation of the degradation machinery remains an unresolved issue. As the 26S proteasome represents the main proteolytic system devoted to the controlled degradation of intracellular proteins, the purpose of the present study was to investigate the functions of this complex in the notothenioid Trematomus bernacchii, in order to better understand its role in the physiology of Antarctic fish. To this aim, we purified and characterized the 26S proteasome from T. bernacchii and isolated the cDNAs codifying seven of the 14 subunits belonging to the proteasome 20S core particle. Results provided evidences of the high resistance of the piscine 26S proteasome to oxidative agents and of its ‘uncommon’ ability to efficiently hydrolyse oxidized bovine serum albumin (BSA), suggesting that this enzymatic complex could play a key role in the antioxidant defense systems in fish inhabiting permanently cold marine environments. These unique properties were also reflected by the 3D model analysis, which revealed a higher structural stability of the piscine complex respect to the murine template. Finally, a comparative analysis, performed in a variety of tissues collected from T. bernacchii and the temperate fish Dicentrarchus labrax, showed a lower protein retention in the cold-adapted fish, possibly due to a better efficiency of its degradation machinery. |
format |
Article in Journal/Newspaper |
author |
Gogliettino, Marta Balestrieri, Marco Riccio, Alessia Facchiano, Angelo Fusco, Carmela Palazzo, Vincenzo Cecere Rossi, Mosè Cocca, Ennio Palmieri, Gianna |
spellingShingle |
Gogliettino, Marta Balestrieri, Marco Riccio, Alessia Facchiano, Angelo Fusco, Carmela Palazzo, Vincenzo Cecere Rossi, Mosè Cocca, Ennio Palmieri, Gianna Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii |
author_facet |
Gogliettino, Marta Balestrieri, Marco Riccio, Alessia Facchiano, Angelo Fusco, Carmela Palazzo, Vincenzo Cecere Rossi, Mosè Cocca, Ennio Palmieri, Gianna |
author_sort |
Gogliettino, Marta |
title |
Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii |
title_short |
Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii |
title_full |
Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii |
title_fullStr |
Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii |
title_full_unstemmed |
Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii |
title_sort |
uncommon functional properties of the first piscine 26s proteasome from the antarctic notothenioid trematomus bernacchii |
publisher |
Portland Press Ltd. |
publishDate |
2016 |
url |
http://dx.doi.org/10.1042/bsr20160022 https://portlandpress.com/bioscirep/article-pdf/doi/10.1042/BSR20160022/477677/bsr036e320.pdf |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Bioscience Reports volume 36, issue 2 ISSN 0144-8463 1573-4935 |
op_rights |
http://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.1042/bsr20160022 |
container_title |
Bioscience Reports |
container_volume |
36 |
container_issue |
2 |
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1810490005890531328 |