2. 植物の凍結耐性と低温誘導蛋白質(セミナー「低温環境への植物の適応-基礎と応用」)

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Cold acclimation processes involve dramatic alterations in protein synthesis and gene expression in a variety of plant species. Most soluble proteins are coagulated by heating at 100℃ for 10 minutes, but some highly hydrophilic cold-regulated proteins (CORs) remain soluble in aqueous solution. In our previous studies, we analyzed heat-stable proteins and their mRNAs during cold acclimation of spinach. Heat-stable COR with a molecular mass of 85 kDa (COR85) was the most evident in levels of protein synthesis and mRNA accumulation among all heat-stable CORs. Increased levels of COR 85 correlated with the development of freezing tolerance during cold acclimation. Interestingly, COR 85 accumulated specifically in the leaves and stems and not roots of the cold-acclimated plants. Consistent with this observation, freezing tolerance was induced in leaves and stems, but not in roots. COR 85 was a member of Group II LEA protein family and inducible by drought, salt stress, and abscisic acid. We obtained evidence that COR 85 is involved in cryoprotection of a freezing-sensitive enzyme. Among the nine proteins with a variety of hydrophilicity, COR 85 was the most effective in protecting against freezing denaturation of lactate dehydrogenase in vitro. On the other hand, some soluble proteins were coimmunoprecipitated with COR 85, suggesting that they may interact with COR 85 in vivo. These data allow us propose the hypothesis that COR 85 may be associated with some stress-sensitive enzymes.
低温生物工学会の論文
1996-07-28

2. 植物の凍結耐性と低温誘導蛋白質(セミナー「低温環境への植物の適応-基礎と応用」)

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