The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions.
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 signa...
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doaj-d01f9dc3ed3b4945819c7ee2ef950ca12020-11-25T01:19:29ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0182e5706110.1371/journal.pone.0057061The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions.Yinnan MuFu-Ming LianYan-Bin TengJingqun AoYong-Liang JiangYong-Xing HeYuxing ChenCong-Zhao ZhouXinhua ChenPeroxiredoxins (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.http://europepmc.org/articles/PMC3581551?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yinnan Mu Fu-Ming Lian Yan-Bin Teng Jingqun Ao Yong-Liang Jiang Yong-Xing He Yuxing Chen Cong-Zhao Zhou Xinhua Chen |
spellingShingle |
Yinnan Mu Fu-Ming Lian Yan-Bin Teng Jingqun Ao Yong-Liang Jiang Yong-Xing He Yuxing Chen Cong-Zhao Zhou Xinhua Chen The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions. PLoS ONE |
author_facet |
Yinnan Mu Fu-Ming Lian Yan-Bin Teng Jingqun Ao Yong-Liang Jiang Yong-Xing He Yuxing Chen Cong-Zhao Zhou Xinhua Chen |
author_sort |
Yinnan Mu |
title |
The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions. |
title_short |
The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions. |
title_full |
The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions. |
title_fullStr |
The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions. |
title_full_unstemmed |
The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions. |
title_sort |
n-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker pseudosciaena crocea is involved in its biological functions. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2013-01-01 |
description |
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. |
url |
http://europepmc.org/articles/PMC3581551?pdf=render |
work_keys_str_mv |
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