Chilling Stress Accelerates Degradation of Seed Storage Protein and Photosynthetic Protein during Cotton Seed Germination
Chilling Stress Accelerates Degradation of Seed Storage Protein and Photosynthetic Protein during Cotton Seed Germination
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DOI：
10.1111/j.1439-037x.2008.00311.x
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发表时间：
2008-08
影响因子：
3.5
通讯作者：
Y. Gai;X. Z. Li;Xianling Ji;Changai Wu;G. Yang;C. Zheng
中科院分区：
文献类型：
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作者：
Y. Gai;X. Z. Li;Xianling Ji;Changai Wu;G. Yang;C. Zheng
低温是限制许多重要作物生产力和地理分布的主要非生物胁迫之一。为了更好地了解棉花（Gossypium hirsutum L.）的低温胁迫反应，我们进行了比较蛋白质组学分析。以4 °C低温处理和未低温处理的1周龄棉花幼苗为材料，提取子叶蛋白质，采用双向凝胶电泳进行分离和比较。在每个凝胶上可重复检测的1500个蛋白质点中，25个蛋白质点下调，29个蛋白质点上调。通过质谱分析鉴定了7种棉花蛋白为β-球蛋白A前体片段。其中一个被鉴定为Rubisco大亚基片段，为低温胁迫对种子贮藏蛋白和光合蛋白的破坏提供了证据。相关生理生化分析表明，低温胁迫下棉花幼苗内肽酶活性和活性氧产生速率显著升高，羧化效率和最大净光合速率明显降低。在此基础上，对低温胁迫下β-球蛋白和Rubisco的降解机理进行了初步探讨。总之，我们的研究提供了新的见解棉花低温胁迫反应，并证明了蛋白质组学分析的优势。
Low temperature is one of the major abiotic stresses limiting the productivity and geographical distribution of many important crops. To gain a better understanding of chilling stress responses in cotton (Gossypium hirsutum L.), we carried out a comparative proteomic analysis. Cotyledon proteins of 1-week-old cotton seedlings treated with or without chilling treatment at 4 °C were extracted, separated by a two-dimensional gel electrophoresis and compared. Among 1500 protein spots reproducibly detected on each gel, 25 protein spots were down-regulated and 29 were up-regulated. Seven cotton proteins were identified by mass spectrometry analysis as beta-globulin A precursor fragments. One was identified as a Rubisco large subunit fragment, providing evidence of both seed storage protein and photosynthetic protein destruction by chilling stress. The related physiological and biochemical analysis showed that there was a significant increase in endopeptidase activity and activated oxygen generation rate, and an obvious decrease in carboxylation efficiency and maximum net photosynthetic rate of cotton seedlings under chilling stress. Based on the above results, the degradation mechanisms of beta-globulin and Rubisco under chilling stress were discussed. In conclusion, our study provides new insights into chilling-stress responses in cotton and demonstrates the advantages of proteomic analysis.