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- Title
The N-Terminal β-Sheet of Peroxiredoxin 4 in the Large Yellow Croaker <i>Pseudosciaena crocea</i> Is Involved in Its Biological Functions.
- Authors
Mu, Yinnan; Lian, Fu-Ming; Teng, Yan-Bin; Ao, Jingqun; Jiang, Yong-Liang; He, Yong-Xing; Chen, Yuxing; Zhou, Cong-Zhao; Chen, Xinhua
- 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 β-sheet that contributes to the dimer interface. Deletion of this β-sheet decreased the in vitro peroxidase activity to about 50% of the wild-type. In vivo assays further demonstrated that removal of this β-sheet led to some impairment in the ability of Prx4 to negatively regulate nuclear factor-κB (NF-κB) 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.
- Subjects
PEROXIREDOXINS; ANTIOXIDANTS; PEROXIDASE; REACTIVE oxygen species; CELLULAR signal transduction; DELETION mutation; BIOLOGICAL assay; PROTEIN structure
- Publication
PLoS ONE, 2013, Vol 8, Issue 2, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0057061