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Seed storage globulins: Origin and evolution of primary and higher order structures

机译：种子储存球蛋白：一级和高级结构的起源和进化

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摘要

Legumin and vicilin are two-domain seed storage globulins similar in primary and higher order structures of their domains to single-domain plant germins as well as to the domains of two-domain and single-domain bacterial oxalate decarboxylases. Independent evolutionary pathways have been shown for the descent of the storage globulins and germins from two-domain and single-domain bacterial oxalate decarboxylases, respectively. As compared to vicilins, the primary and tertiary structures of legumins were found to most closely reflect the ancient features characteristic of a common precursor of storage globulins. During the evolution of the storage globulins, a mechanism specifically controlling their degradation has been formed. We found that limited proteolysis of soybean legumin and kidney bean vicilin in germinating seeds and in vitro leads to their regular changes, which initiate an extensive cleavage of storage globulin molecules by the one-by-one mechanism. As also shown, limited proteolysis of soybean legumin loosens the intersubunit interactions in its oligomeric molecule. Based on these data, we hypothesize that the deep one-by-one degradation of soybean legumin is triggered by its dissociation, which bares peptide bonds potentially susceptible to proteolytic attack but are masked in the oligomer.
机译：豆蛋白和豌豆球蛋白是两结构域的种子存储球蛋白，其结构域的一级和高级结构类似于单结构域植物种质蛋白以及两结构域和单结构域细菌草酸盐脱羧酶的结构域。已经显示出独立的进化途径可分别从二域和单域细菌草酸盐脱羧酶中分离出存储球蛋白和胚芽。与豆荚蛋白相比，豆荚蛋白的一级和三级结构最能反映出常见的贮存球蛋白前体的古代特征。在储存球蛋白的进化过程中，已经形成了专门控制其降解的机制。我们发现大豆豆豆蛋白和芸豆豌豆球蛋白在发芽种子中的有限蛋白水解作用和体外作用导致它们的规律性变化，从而通过一对一的机制引发广泛的储存球蛋白分子裂解。还如图所示，大豆豆蛋白的有限的蛋白水解作用使其寡聚分子中的亚基间相互作用松散。基于这些数据，我们假设大豆豆蛋白的深度一对一降解是由其解离引发的，解离裸露了可能易受蛋白水解攻击的肽键，但在寡聚物中被掩盖了。

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