STRUCTURAL-CHANGES IN THYLAKOID PROTEINS DURING COLD-ACCLIMATION AND FREEZING OF WINTER RYE (SECALE-CEREALE L-CV PUMA)
STRUCTURAL-CHANGES IN THYLAKOID PROTEINS DURING COLD-ACCLIMATION AND FREEZING OF WINTER RYE (SECALE-CEREALE L-CV PUMA)
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DOI：
10.1104/pp.70.2.418
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发表时间：
1982-01-01
期刊：
影响因子：
7.4
通讯作者：
HUNER, NPA
中科院分区：
文献类型：
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作者：
GRIFFITH, M;BROWN, GN;HUNER, NPA
从非硬化和冷硬化的冬黑麦中分离出类囊体。燕麦属CV. Puma），并在存在和不存在氢基试剂的情况下进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳[SDS-PAGE]。冷硬化黑麦类囊体蛋白的电泳揭示了存在的35千道尔顿[Kd]多肽和51 Kd的多肽中发现nonhardened黑麦类囊体蛋白的情况下。35 Kd带可以通过加入β-巯基乙醇的非硬化黑麦类囊体蛋白，而51 Kd带可以通过添加铜菲咯啉这些相同的蛋白质形成。巯基滴定表明，冷硬化黑麦类囊体蛋白含有更多的游离巯基比nonhardened黑麦蛋白。虽然类囊体蛋白质的氨基酸分析显示在几个氨基酸残基的数量差异，极性的类囊体蛋白质没有改变在冷驯化。无论是非硬化或冷硬化植物在体内或体外冷冻时，类囊体蛋白的SDS-PAGE凝胶没有显着变化。当在β-葡萄糖存在下冷冻时，类囊体蛋白确实聚集。巯基乙醇虽然类囊体蛋白从冷硬化黑麦中分离出含有更多的还原硫醇，一般状态的还原并没有作为冷冻保护剂。特定蛋白质的构象变化可能对黑麦低温生长具有重要意义。
Thylakoids were isolated from nonhardened and cold-hardened winter rye (S. cereale L. cv. Puma), and subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis [SDS-PAGE] in the presence and absence of sylfhydryl reagents. Electrophoresis of cold-hardened rye thylakoid proteins revealed the presence of a 35 kilodalton [Kd] polypeptide and the absence of a 51 Kd polypeptide found in nonhardened rye thylakoid proteins. The 35 Kd band could be induced by adding .beta.-mercaptoethanol to nonhardened rye thylakoid proteins, whereas the 51 Kd band could be formed by adding cupric phenanthroline to these same proteins. Sulfhydryl group titration showed that cold-hardened rye thylakoid proteins contained more free sulfhydryls than nonhardened rye proteins. Although amino acid analysis of thylakoid proteins revealed quantitative differences in several amino acid residues, the polarity of thylakoid proteins did not change during cold acclimation. No significant change in SDS-PAGE gels of thylakoid proteins appeared when either nonhardened or cold-hardened plants were frozen in vivo or in vitro. Thylakoid proteins did aggregate when frozen in the presence of .beta.-mercaptoethanol. Although thylakoid proteins isolated from cold-hardened rye contained more reduced thiols, a general state of reduction did not act as a cryoprotectant. Conformational changes of specific proteins may be important for low temperature growth of rye.