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首页> 外文期刊>Biochemistry >Identification and activity of a lower eukaryotic serine proteinase inhibitor (serpin) from Cyanea capillata: Analysis of a jellyfish serpin, jellypin
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Identification and activity of a lower eukaryotic serine proteinase inhibitor (serpin) from Cyanea capillata: Analysis of a jellyfish serpin, jellypin

机译：Cyanea capillata的一种低等真核丝氨酸蛋白酶抑制剂（serpin）的鉴定和活性：水母丝氨酸蛋白酶抑制剂，水母蛋白的分析

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摘要

Delineating the phylogenetic relationships among members of a protein family can provide a high degree of insight into the evolution of domain structure and function relationships. To identify an early metazoan member of the high molecular weight serine proteinase inhibitor (serpin) superfamily, we initiated a cDNA library screen of the cnidarian, Cyanea capillata. We identified one serpin cDNA encoding for a full-length serpin, jellypin. Phylogenetic analysis using the deduced amino acid sequence showed that jellypin was most similar to the platyhelminthe Echinococcus multiocularis serpin and the clade P serpins, suggesting that this serpin evolved similar to1000 million years ago (MYA). Modeling of jellypin showed that it contained all the functional elements of an inhibitory serpin. In vitro biochemical analysis confirmed that jellypin was an inhibitor of the S1 clan SA family of serine proteinases. Analysis of the interactions between the human serine proteinases, chymotrypsin, cathepsin G, and elastase, showed that jellypin inhibited these enzymes in the classical serpin manner, forming a SDS stable enzyme/inhibitor complex. These data suggest that the coevolution of serpin structure and inhibitory function date back to at least early metazoan evolution, similar to1000 MYA.
机译：描绘蛋白质家族成员之间的系统发育关系可以提供对结构域结构和功能关系进化的高度了解。为了确定高分子量丝氨酸蛋白酶抑制剂（丝氨酸蛋白酶抑制剂）超家族的早期后生成员，我们启动了刺胞鱼Cyanea capillata的cDNA文库筛选。我们确定了一种编码全长丝氨酸蛋白酶抑制剂，jellypin的丝氨酸蛋白酶抑制剂cDNA。使用推导的氨基酸序列进行的系统发育分析表明，果冻蛋白与桔梗棘球chin和丝支P丝氨酸最相似，表明这种丝氨酸蛋白酶的进化与十亿年前（MYA）相似。果冻针的建模表明它包含抑制性丝氨酸蛋白酶抑制剂的所有功能元件。体外生化分析证实，果冻素是丝氨酸蛋白酶S1家族SA家族的抑制剂。对人丝氨酸蛋白酶，胰凝乳蛋白酶，组织蛋白酶G和弹性蛋白酶之间相互作用的分析表明，果冻素以经典的丝氨酸蛋白酶抑制方式抑制了这些酶，形成了SDS稳定的酶/抑制剂复合物。这些数据表明丝氨酸蛋白酶抑制剂结构和抑制功能的共同进化至少可以追溯到后生动物早期进化，类似于1000 MYA。

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