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Plant and Cell Physiology Advance Access published online on June 11, 2009
Plant and Cell Physiology, doi:10.1093/pcp/pcp074
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© The Author 2009. 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

Mitochondrial damage in soybean seed axis during imbibition at chilling temperatures

Guangkun Yin1,2, Hongmei Sun1,2, Xia Xin1,2, Guozheng Qin3, Zheng Liang1 and Xinming Jing1,*

1Laboratory of Seed Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China
2Graduate School of Chinese Academy of Sciences, Beijing 100039, China
3Key Laboratory of Photosynthesis and Environmental Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China

Corresponding Author: Prof. Xinming Jing, Telephone: 0086-10-62836009, Fax: 0086-10-62836009, E-mail: xmjing{at}ibcas.ac.cn, Present address: Institute of Botany, Chinese Academy of Sciences, Xiangshan, Beijing, China, 100093


  Abstract

The development of mitochondria during seed germination is essential for plant growth. However, the developmental process is still poorly understood. The temperature plays a key role for soybean germination and in this study we characterized the mitochondrial ultrastructure and proteome after imbibition at 22°C, 10°C and 4°C for 24 h. The mitochondria from the soybean seed axis can be divided into light and heavy mitochondria by Percoll density gradient centrifugation. The 4°C-imbibed axes mainly contained light mitochondria, which had lower levels of specific mitochondrial enzymes and oxidative phosphorylation activity. In contrast, the 22°C-imbibed axes mainly contained heavy mitochondria, which exhibited higher metabolism. Electron microscopy revealed that mitochondria in the 4°C-imbibed axes had a poorly developed internal membrane system with few cristae, while the mitochondria in the 22°C-imbibed axis developed more normally. Furthermore, we compared the axis mitochondrial proteomes during imbibition at different temperature. The differentially expressed proteins were identified using ESI-Q-TOF-MS/MS. Proteins involved in mitochondrial metabolites including malate dehydrogenase (tricarboxylic acid cycle enzyme), putative ATP synthase subunit (oxidative phosphorylation complex subunits), mitochondrial chaperonin-60 (heat shock protein), arginase (urea cycle enzyme), and mitochondrial elongation factor Tu (mitochondrial genome transcript enzyme) were identified. The reduced expression of these proteins might not support the normal mitochondrial metabolism. We conclude that chilling during imbibition causes mitochondrial damage at ultrastructural and metabolic levels.

Keywords: Glycine max (L.) Merr. - imbibition - mitochondria - proteome - ultrastructure

(Received April 16, 2009; Accepted May 25, 2009)
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