Format

Send to

Choose Destination
Int J Mol Sci. 2017 Jul 25;18(8). pii: E1605. doi: 10.3390/ijms18081605.

Unusual Antioxidant Properties of 26S Proteasome Isolated from Cold-Adapted Organisms.

Author information

1
Institute of Biosciences and BioResources, National Research Council (CNR-IBBR), Via Pietro Castellino 111, 80131 Napoli, Italy. marta.gogliettino@ibbr.cnr.it.
2
Institute of Biosciences and BioResources, National Research Council (CNR-IBBR), Via Pietro Castellino 111, 80131 Napoli, Italy. ennio.cocca@ibbr.cnr.it.
3
Institute of Biosciences and BioResources, National Research Council (CNR-IBBR), Via Pietro Castellino 111, 80131 Napoli, Italy. carmela.fusco@ibbr.cnr.it.
4
Institute of Biosciences and BioResources, National Research Council (CNR-IBBR), Via Pietro Castellino 111, 80131 Napoli, Italy. bruna.agrillo@ibbr.cnr.it.
5
Institute of Biosciences and BioResources, National Research Council (CNR-IBBR), Via Pietro Castellino 111, 80131 Napoli, Italy. alessia.riccio@ibbr.cnr.it.
6
Institute of Biosciences and BioResources, National Research Council (CNR-IBBR), Via Pietro Castellino 111, 80131 Napoli, Italy. marco.balestrieri@ibbr.cnr.it.
7
Institute of Food Sciences, National Research Council (CNR-ISA), Via Roma 64, 83100 Avellino, Italy. angelo.facchiano@isa.cnr.it.
8
Institute of Biosciences and BioResources, National Research Council (CNR-IBBR), Via Pietro Castellino 111, 80131 Napoli, Italy. antonio.pepe@ibbr.cnr.it.
9
Institute of Biosciences and BioResources, National Research Council (CNR-IBBR), Via Pietro Castellino 111, 80131 Napoli, Italy. gianna.palmieri@ibbr.cnr.it.

Abstract

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.

KEYWORDS:

26S proteasome; Antarctic fish; antioxidant functions; cold-adaptation; oxidative stress; oxidized protein degradation

PMID:
28757562
PMCID:
PMC5577997
DOI:
10.3390/ijms18081605
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Multidisciplinary Digital Publishing Institute (MDPI) Icon for PubMed Central
Loading ...
Support Center