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Plant and Cell Physiology Advance Access published online on October 22, 2007
Plant and Cell Physiology, doi:10.1093/pcp/pcm143
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© The Author 2007. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Role of the Methionine Sulfoxide Reductase MsrB3 in Cold Acclimation in Arabidopsis

Sun Jae Kwon, Soon Il Kwon, Min Seok Bae1, Eun Ju Cho2 and Ohkmae K. Park*

School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea

Corresponding author: Ohkmae K. Park, School of Life Sciences and Biotechnology, Korea University, Anam-dong, Seongbuk-gu, Seoul 136-701, Korea, Phone) 82-2-3290-3458, Fax) 82-2-3291-3458, E-mail) omkim{at}korea.ac.kr


  Abstract

Methionine residues of proteins are a major target for oxidation by reactive oxygen species (ROS), which are generated in response to a variety of stress conditions. Methionine sulfoxide (MetO) reductases are present in most organisms and play protective roles in the cellular response to oxidative stress, reducing oxidized MetO back to Met. Previously, an Arabidopsis MetO reductase, MsrB3, was identified as a cold-responsive protein (Bae et al. 2003). Here we report that MsrB3 functions in the process of cold acclimation, thus contributing to cold tolerance. In contrast to normal, wild type plants, msrb3 mutant plants lost the ability to become tolerant to freezing temperatures following cold pretreatment. Furthermore, when exposed to low temperature, msrb3 plants exhibited a larger increase in MetO and H2O2 content and electrolyte leakage compared to wild type and MsrB3 transgenic plants. It is also shown that MsrB3 is localized at the endoplasmic reticulum (ER). We propose that MsrB3 plays an important role in cold tolerance by eliminating MetO and ROS that accumulate at the ER during cold acclimation.

Keywords: Arabidopsis - Cold acclimation - Cold stress - Met sulfoxide reductase - Oxidative stress - Reactive oxygen species

1 Present address: Gwangju Regional Korea Food & Drug Administration (KFDA), Gwangju 500-480, Korea.

2 Present address: Department of Molecular Bioscience & Bioengineering, University of Hawaii at Manoa, Honolulu 96822, USA.

(Received September 11, 2007; Accepted October 17, 2007)
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[Abstract] [Full Text] [PDF]


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