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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The ovalbumin serpins revisited: Perspective from the chicken genome of clade B serpin evolution in vertebrates
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The ovalbumin serpins revisited: Perspective from the chicken genome of clade B serpin evolution in vertebrates

机译：卵白蛋白丝氨酸蛋白酶抑制剂再访：脊椎动物进化枝B丝氨酸蛋白酶抑制剂鸡基因组的视角

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摘要

Serpin superfamily proteins, most of which are serine protease inhibitors, share an unusual mechanism rooted in their conserved metastable tertiary structure. Although serpins have been identified in isolated members of archea, bacteria, and plants, a remarkable expansion is found in vertebrates. The chicken protein ovalbumin, a storage protein from egg white, lacking protease inhibitory activity, is an historical member of the superfamily and the founding member of the subgroup known as ov-serpins (ovalbum in-related serpins) or clade B serpins. In the human, ov-serpins include 13 proteins involved in the regulation of inflammation, apoptosis, angiogenesis, and embryogenesis. Here, a detailed analysis of the chicken (Gallus gallus) genome identified 10 clade B serpin genes that map to a single ≈150-kb locus and contain the signature protein sequence of serpins and the gene structure of ov-serpins, with either seven or eight exons. Orthologues of PAI-2 (SERPINB2), MNEI (SERPINB1), PI-6 (SERPINB6), and maspin (SERPINB5) are highly conserved. Comparison with human ov-serpins identified avian-specific and mammal-specific genes. Importantly, a unique model of mammalian ov-serpin evolution is revealed from the comparative analysis of the chicken and human loci. The presence of a subset of ov-serpin genes in zebrafish (Danio rerio) gives insight into the ancestral locus. This comparative genomic study provides a valuable perspective on the evolutionary pathway for the clade B serpins, allowing the identification of genes with functions that may have been conserved since the origin of vertebrates. In addition, it suggests that "newer" serpins, such as ovalbumin, have contributed to vertebrate adaptation.
机译：丝氨酸蛋白酶抑制剂超家族蛋白，其中大多数是丝氨酸蛋白酶抑制剂，共有一个不寻常的机制，其根源在于其保守的亚稳态三级结构。尽管在古细菌，细菌和植物的分离成员中发现了丝氨酸蛋白酶抑制剂，但在脊椎动物中却发现了显着的扩展。鸡蛋白卵清蛋白是卵清蛋白中的一种蛋白，缺乏蛋白酶抑制活性，是超家族的历史成员，也是ov-serpins（与卵子相关的serpins）或进化枝B serpins的创始成员。在人类中，ov-serpins包含13种蛋白质，参与炎症，细胞凋亡，血管生成和胚胎发生的调控。在这里，对鸡（鸡鸡）基因组的详细分析确定了10个进化枝B丝氨酸蛋白酶抑制剂基因，这些基因映射到单个≈150kb的基因座，并包含丝氨酸蛋白酶抑制剂的特征蛋白序列和ov-丝氨酸蛋白酶抑制剂的基因结构，其中有7个或八个外显子。 PAI-2（SERPINB2），MNEI（SERPINB1），PI-6（SERPINB6）和maspin（SERPINB5）的直系同源物高度保守。与人ov-serpins的比较确定了禽特异性和哺乳动物特异性基因。重要的是，通过对鸡和人基因座的比较分析揭示了哺乳动物ov-serpin进化的独特模型。斑马鱼（Danio rerio）中存在ov-serpin基因子集，可以深入了解祖先的基因座。这项比较基因组研究为进化枝B型丝氨酸蛋白酶抑制剂的进化途径提供了宝贵的见解，从而可以鉴定出自脊椎动物起源以来具有保守功能的基因。另外，它表明“较新的”丝氨酸蛋白酶抑制蛋白，例如卵清蛋白，已经促进了脊椎动物的适应。

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