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Cited 10 time in webofscience Cited 10 time in scopus
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Molecular and functional properties of three different peroxiredoxin isotypes in Chinese cabbageopen access

Authors
Kim, Sun YoungJung, Young JunShin, Mi RimPark, Jung HoonNawkar, Ganesh M.Maibam, PunyakishoreLee, Eun SeonKim, Kang-SanPaeng, Seol KiKim, Woe YeonLee, Kyun OhYun, Dae-JinKang, Chang HoLee, Sang Yeol
Issue Date
Jan-2012
Publisher
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
Keywords
chaperone; peroxidase; plant peroxiredoxin
Citation
MOLECULES AND CELLS, v.33, no.1, pp 27 - 33
Pages
7
Indexed
SCI
SCIE
SCOPUS
KCI
Journal Title
MOLECULES AND CELLS
Volume
33
Number
1
Start Page
27
End Page
33
URI
https://scholarworks.gnu.ac.kr/handle/sw.gnu/22429
DOI
10.1007/s10059-012-2166-8
ISSN
1016-8478
0219-1032
Abstract
Peroxiredoxins (Prxs), which are classified into three isotypes in plants, play important roles in protection systems as peroxidases or molecular chaperones. The three Prx isotypes of Chinese cabbage, namely C1C-Prx, C2C-Prx, and C-PrxII, have recently been identified and characterized. The present study compares their molecular properties and biochemical functions to gain insights into their concerted roles in plants. The three Prx isotype genes were differentially expressed in tissue- and developmental stage-specific manners. The transcript level of the C1C-Prx gene was abundant at the seed stage, but rapidly decreased after imbibitions. In contrast, the C2C-Prx transcript was not detected in the seeds, but its expression level increased at germination and was maintained thereafter. The C-PrxII transcript level was mild at the seed stage, rapidly increased for 10 days after imbibitions, and gradually disappeared thereafter. In the localization analysis using GFP-fusion proteins, the three isotypes showed different cellular distributions. C1C-Prx was localized in the cytosol and nucleus, whereas C2C-Prx and C-Prx were found mainly in the chloroplast and cytosol, respectively. In vitro thiol-dependent antioxidant assays revealed that the relative peroxidase activities of the isotypes were CPrxII > C2C-Prx > C1C-Prx. C1C-Prx and C2C-Prx, but not C-PrxII, prevented aggregation of malate dehydrogenase as a molecular chaperone. Taken together, these results suggest that the three isotypes of Prx play specific roles in the cells in timely and spatially different manners, but they also cooperate with each other to protect the plant.
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