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首页> 外文期刊>Zoological Science >Purification and Characterization of Coacervate-Forming Cuticular Proteins from Papilio xuthus Pupae
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Purification and Characterization of Coacervate-Forming Cuticular Proteins from Papilio xuthus Pupae

机译：api（Papilio xuthus up）中形成凝聚层的表皮蛋白的纯化和鉴定

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The Papilio xuthus (Lepidoptera: Papilionidae) pupa expresses novel soluble proteins that undergo reversible temperature-dependent coacervate-formation. We purified two coacervate-forming proteins, PX-1 and PX-4, from the wings of pharate adults. PX-1 and PX-4 form coacervates upon warming. Transmission electron microscopy analysis revealed that these proteins assemble ordered bead-like ultrastructures. We cloned and sequenced PX-1 and PX-4 cDNAs. The PX-1 and PX-4 amino acid sequences contain many hydrophobic residues and show homologies to insect cuticular proteins. Moreover, when recombinant PX-1 and PX-4 were overexpressed in Escherichia coli, both recombinant proteins exhibited temperature-dependent coacervation. Furthermore, analyses of truncated mutants of PX-1 suggest that both the Val/Pro-rich region and Gly/Ile-rich regions of PX-1 are involved in such coacervation.
机译：Papilio xuthus（鳞翅目：Papilionidae）pa表达可溶的蛋白质，这些蛋白质经过可逆的温度依赖性凝聚形成。我们从噬菌体成虫的翅膀中纯化了两种凝聚形成蛋白PX-1和PX-4。 PX-1和PX-4在升温时会形成凝聚层。透射电镜分析表明，这些蛋白质组装有序的珠状超微结构。我们克隆并测序了PX-1和PX-4 cDNA。 PX-1和PX-4氨基酸序列包含许多疏水残基，并与昆虫表皮蛋白同源。此外，当重组PX-1和PX-4在大肠杆菌中过表达时，两种重组蛋白都表现出温度依赖性凝聚。此外，对PX-1截短突变体的分析表明，PX-1的Val / Pro富集区和Gly / Ile富集区都参与了这种凝聚。

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