| Registro completo |
| Provedor de dados: |
OAK
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| País: |
Japan
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| Título: |
Identification and functional analysis of a novel mitochondria-localized 2-Cys peroxiredoxin, BbTPx-2, from Babesia bovis
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| Autores: |
Masatani, Tatsunori
Asada, Masahito
Hakimi, Hassan
Hayashi, Kei
Yamagishi, Junya
Kawazu, Shin-ichiro
Xuan, Xuenan
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| Data: |
2016-08
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| Ano: |
2016
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| Palavras-chave: |
Antioxidant activity
Babasia bovis
Mitochondria
Peroxiredoxin
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| 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.
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| Idioma: |
Inglês
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| Identificador: |
http://ir.obihiro.ac.jp/dspace/handle/10322/4487
info:doi/10.1007/s00436-016-5071-9
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| Editor: |
Springer
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| Direitos: |
The final publication is available at Springer via http://doi.org/10.1007/s00436-016-5071-9.
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