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Mol. Cells 2012; 33(1): 27-33

Published online January 31, 2012

https://doi.org/10.1007/s10059-012-2166-8

© The Korean Society for Molecular and Cellular Biology

Molecular and Functional Properties of Three Different Peroxiredoxin Isotypes in Chinese Cabbage

Sun Young Kim1,2, Young Jun Jung1,2, Mi Rim Shin1,2, Jung Hoon Park1, Ganesh M. Nawkar1, Punyakishore Maibam1, Eun Seon Lee1, Kang-San Kim1, Seol Ki Paeng1, Woe Yeon Kim1, Kyun Oh Lee1, Dae-Jin Yun1, Chang Ho Kang1,*, and Sang Yeol Lee1,*

1Division of Applied Life Sciences (Brain Korea 21 program), Gyeongsang National University, Jinju 660-701, Korea, 2These authors contributed equally to this work.

Correspondence to : *Correspondence: sylee@gnu.ac.kr (SYL); jacobgnu69@gnu.ac.kr (CHK)

Received: August 16, 2011; Revised: November 30, 2011; Accepted: December 8, 2011

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 C-PrxII > 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.

Keywords chaperone, peroxidase, plant peroxiredoxin

Article

Research Article

Mol. Cells 2012; 33(1): 27-33

Published online January 31, 2012 https://doi.org/10.1007/s10059-012-2166-8

Copyright © The Korean Society for Molecular and Cellular Biology.

Molecular and Functional Properties of Three Different Peroxiredoxin Isotypes in Chinese Cabbage

Sun Young Kim1,2, Young Jun Jung1,2, Mi Rim Shin1,2, Jung Hoon Park1, Ganesh M. Nawkar1, Punyakishore Maibam1, Eun Seon Lee1, Kang-San Kim1, Seol Ki Paeng1, Woe Yeon Kim1, Kyun Oh Lee1, Dae-Jin Yun1, Chang Ho Kang1,*, and Sang Yeol Lee1,*

1Division of Applied Life Sciences (Brain Korea 21 program), Gyeongsang National University, Jinju 660-701, Korea, 2These authors contributed equally to this work.

Correspondence to:*Correspondence: sylee@gnu.ac.kr (SYL); jacobgnu69@gnu.ac.kr (CHK)

Received: August 16, 2011; Revised: November 30, 2011; Accepted: December 8, 2011

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 C-PrxII > 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.

Keywords: chaperone, peroxidase, plant peroxiredoxin

Mol. Cells
Sep 30, 2022 Vol.45 No.9, pp. 603~672
COVER PICTURE
The Target of Rapamycin Complex (TORC) is a central regulatory hub in eukaryotes, which is well conserved in diverse plant species, including tomato (Solanum lycopersicum). Inhibition of TORC genes (SlTOR, SlLST8, and SlRAPTOR) by VIGS (virus-induced gene silencing) results in early fruit ripening in tomato. The red/ orange tomatoes are early-ripened TORC-silenced fruits, while the green tomato is a control fruit. Top, left, control fruit (TRV2-myc); top, right, TRV2-SlLST8; bottom, left, TRV2-SlTOR; bottom, right, TRV2-SlRAPTOR(Choi et al., pp. 660-672).

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