翻译后修饰切割在大豆球蛋白组装中的作用。
Role of posttranslational cleavage in glycinin assembly.
作者信息
Dickinson C D, Hussein E H, Nielsen N C
机构信息
United States Department of Agriculture/Agricultural Research Service, Purdue University, West Lafayette, Indiana 47907.
出版信息
Plant Cell. 1989 Apr;1(4):459-69. doi: 10.1105/tpc.1.4.459.
Abstract
Glycinin, like other 11S seed storage proteins, undergoes a complex series of posttranslational events between the time proglycinin precursors are synthesized in endoplasmic reticulum and the mature glycinin subunits are deposited in vacuolar protein bodies. According to the current understanding of this process, proglycinin subunits aggregate into trimers in endoplasmic reticulum, and then the trimers move to the vacuolar protein bodies where a protease cleaves them into acidic and basic polypeptide chains. Stable glycinin hexamers, rather than trimers, are isolated from mature seeds. We used a re-assembly assay in this study to demonstrate that proteolytic cleavage of the proglycinin subunits is required for in vitro assembly of glycinin oligomers beyond the trimer stage. The possibility that the cleavage is a regulatory step and that it triggers the deposition of 11S seed storage proteins as insoluble aggregates in vivo is considered.
摘要
大豆球蛋白与其他11S种子贮藏蛋白一样，在大豆球蛋白前体在内质网中合成到成熟的大豆球蛋白亚基沉积到液泡蛋白体的过程中，经历了一系列复杂的翻译后事件。根据目前对这一过程的理解，大豆球蛋白前体亚基在内质网中聚合成三聚体，然后三聚体移动到液泡蛋白体，在那里一种蛋白酶将它们切割成酸性和碱性多肽链。从成熟种子中分离出的是稳定的大豆球蛋白六聚体，而不是三聚体。在本研究中，我们使用了一种重组测定法来证明，大豆球蛋白亚基的蛋白水解切割是三聚体阶段以上大豆球蛋白寡聚体体外组装所必需的。我们考虑了这种切割是一个调节步骤并触发11S种子贮藏蛋白在体内以不溶性聚集体形式沉积的可能性。
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