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The N-terminal ?-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions.


ABSTRACT: Peroxiredoxins (Prxs) are thiol-specific antioxidant proteins that exhibit peroxidase and peroxynitrite reductase activities involved in the reduction of reactive oxygen species. The peroxiredoxin Prx4 from the large yellow croaker Pseudosciaena crocea is a typical 2-Cys Prx with an N-terminal signal peptide. We solved the crystal structure of Prx4 at 1.90 Å and revealed an N-terminal antiparallel ?-sheet that contributes to the dimer interface. Deletion of this ?-sheet decreased the in vitro peroxidase activity to about 50% of the wild-type. In vivo assays further demonstrated that removal of this ?-sheet led to some impairment in the ability of Prx4 to negatively regulate nuclear factor-?B (NF-?B) activity and to perform its role in anti-bacterial immunity. These results provide new insights into the structure and function relationship of a peroxiredoxin from bony fish.

SUBMITTER: Mu Y 

PROVIDER: S-EPMC3581551 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions.

Mu Yinnan Y   Lian Fu-Ming FM   Teng Yan-Bin YB   Ao Jingqun J   Jiang Yong-Liang YL   He Yong-Xing YX   Chen Yuxing Y   Zhou Cong-Zhao CZ   Chen Xinhua X  

PloS one 20130225 2


Peroxiredoxins (Prxs) are thiol-specific antioxidant proteins that exhibit peroxidase and peroxynitrite reductase activities involved in the reduction of reactive oxygen species. The peroxiredoxin Prx4 from the large yellow croaker Pseudosciaena crocea is a typical 2-Cys Prx with an N-terminal signal peptide. We solved the crystal structure of Prx4 at 1.90 Å and revealed an N-terminal antiparallel β-sheet that contributes to the dimer interface. Deletion of this β-sheet decreased the in vitro pe  ...[more]

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