Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS
Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS
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DOI：
10.1073/pnas.1114052109
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发表时间：
2012-04-03
影响因子：
11.1
通讯作者：
Sunde, Margaret
中科院分区：
文献类型：
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作者：
Macindoe, Ingrid;Kwan, Ann H.;Sunde, Margaret
来自真菌粗糙脉孢菌的疏水蛋白EAS形成称为小棒的功能性淀粉样纤维，其促进孢子形成和分散。EAS自组装成纤维状小棒自发发生在疏水：亲水界面和小棒进一步关联横向形成两亲性单分子膜。我们已经使用了定点诱变和肽实验，以确定该地区的EAS驱动分子间的协会和形成的交叉β小棒结构。将该区域移植到非淀粉样疏水蛋白中使其能够形成小棒。我们还确定了EAS变体的结构和动力学，其具有降低的小棒形成能力。两者合计，这些数据使我们能够精确定位的构象变化时发生的疏水蛋白自组装在一个接口，并提出了一个模型的两亲性EAS棒结构。
The hydrophobin EAS from the fungus Neurospora crassa forms functional amyloid fibrils called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar rodlets occurs spontaneously at hydrophobic: hydrophilic interfaces and the rodlets further associate laterally to form amphipathic monolayers. We have used site-directed mutagenesis and peptide experiments to identify the region of EAS that drives intermolecular association and formation of the cross-beta rodlet structure. Transplanting this region into a nonamyloidogenic hydrophobin enables it to form rodlets. We have also determined the structure and dynamics of an EAS variant with reduced rodlet-forming ability. Taken together, these data allow us to pinpoint the conformational changes that take place when hydrophobins self-assemble at an interface and to propose a model for the amphipathic EAS rodlet structure.