EsTrx-2, the mitochondrial thioredoxin from Antarctic microcrustacean (Euphausia superba): Cloning and functional characterization.
Comp Biochem Physiol B Biochem Mol Biol
; 231: 52-58, 2019 May.
Article
em En
| MEDLINE
| ID: mdl-30776436
ABSTRACT
Thioredoxin system plays an important role in antioxidative stress, thioredoxin 2 (Trx2) being one of the most important components in the thioredoxin system. The full-length cDNA sequence of thioredoxin 2 from Euphausia superba (EsTrx2) is 1276â¯bp and contain a 5' untranslated region (UTR) of 94â¯bp, a 3' UTR of 741â¯bp and an open reading frame (ORF) of 441â¯bp, encoding a putative protein of 146 amino acids. Multiple sequence alignments have indicated that EsTrx2 possesses a conserved (-Cys-Gly-Pro-Cys-) CGPC redox-active site. EsTrx2 shares 62.3% identity with the swimming crab (Portunus trituberculatus) Trx2. The predicted three-dimensional structure of EsTrx2 consists of a thioredoxin fold. The high similarity and phylogenetic analysis have indicated that EsTrx2 is a member of the mitochondrial Trx2 sub-family. The recombinant EsTrx2 (rEsTrx2) was constructed and expressed in Escherichia coli BL21 (DE3). The rEsTrx2 protein showed high redox activity and antioxidant capacity at temperature from 4 to 37⯰C. All results indicated that EsTrx2 was involved in the oxidative stress response of E. superba.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Tiorredoxinas
/
Regulação da Expressão Gênica
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Euphausiacea
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Mitocôndrias
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
Comp Biochem Physiol B Biochem Mol Biol
Assunto da revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Ano de publicação:
2019
Tipo de documento:
Article