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Provedor de dados:  OAK
País:  Japan
Título:  Identification and functional analysis of a novel mitochondria-localized 2-Cys peroxiredoxin, BbTPx-2, from Babesia bovis
Autores:  Masatani, Tatsunori
Asada, Masahito
Hakimi, Hassan
Hayashi, Kei
Yamagishi, Junya
Kawazu, Shin-ichiro
Xuan, Xuenan
Data:  2016-08
Ano:  2016
Palavras-chave:  Antioxidant activity
Babasia bovis
Resumo:  Cysteine-based peroxidases, known as peroxiredoxins (Prx) or thioredoxin peroxidases (TPx), are important antioxidant enzymes that prevent oxidative damage caused by reactive oxygen species (ROS). In this study, we identified a novel mitochondrial 2-Cys Prx, BbTPx-2, from a bovine Babesia parasite, B. bovis. BbTPx-2 complementary DNA (cDNA) encodes a polypeptide of 254 amino acid residues. This protein has a mitochondrial targeting peptide at the N-terminus and two conserved cysteine residues of the typical 2-Cys Prx. By using a thiol mixed-function oxidation assay, the antioxidant activity of recombinant BbTPx-2 was revealed, and its antioxidant activity was comparable to that of a cytosolic 2-Cys Prx from B. bovis, BbTPx-1. Notably, we confirmed that BbTPx-2 was expressed in the mitochondrion of B. bovis merozoites. Taken together, the results suggest that the mitochondrial BbTPx-2 is an antioxidative enzyme for scavenging ROS in B. bovis.
Idioma:  Inglês

Editor:  Springer
Direitos:  The final publication is available at Springer via

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