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首页> 外文期刊>Biochemistry >Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry.
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Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry.

机译：通过氢/氘交换和质谱法分析an的HET-s蛋白的淀粉样蛋白聚集时发生的构象转变。

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摘要

The [Het-s] infectious element of the filamentous fungus Podospora anserina corresponds to the prion form of the HET-s protein. HET-s (289 amino acids in length) aggregates into amyloid fibers in vitro. Such fibers obtained in vitro are infectious, indicating that the [Het-s] prion can propagate as a self-perpetuating amyloid aggregate of the HET-s protein. Previous analyses have suggested that only a limited region of the HET-s protein is involved in amyloid formation and prion propagation. To document the conformational transition occurring upon amyloid aggregation of HET-s, we have developed a method involving hydrogen/deuterium exchange monitored by MALDI-MS. In a first step, a peptide mass fingerprint of the protein was obtained, leading to 87% coverage of the HET-s primary structure. Amyloid aggregates of HET-s were obtained, and H/D exchange was monitored on the soluble and on the amyloid form of HET-s. This study revealed that in the soluble form of HET-s, the C-terminal region (spanning from residues 240-289) displays a high solvent accessibility. In sharp contrast, solvent accessibility is drastically reduced in that region in the amyloid form. H/D exchange rates and levels in the N-terminal part of the protein (residues 1-220) are comparable in the soluble and the aggregated state. These results indicate that amyloid aggregation of HET-s involves a conformational transition of the C-terminal part of the protein from a mainly disordered to an aggregated state in which this region is highly protected from hydrogen exchange.
机译：丝状真菌Podospora anserina的[Het-s]感染元件对应于HET-s蛋白的病毒形式。 HET-s（长度为289个氨基酸）在体外聚集成淀粉样纤维。体外获得的此类纤维具有感染力，表明[Het-s] ion病毒可以作为HET-s蛋白的自持久淀粉样蛋白聚集体繁殖。先前的分析表明，HET-s蛋白只有有限的区域参与淀粉样蛋白的形成和病毒的繁殖。为了记录在HET-s的淀粉样蛋白聚集时发生的构象转变，我们开发了一种涉及通过MALDI-MS监测氢/氘交换的方法。第一步，获得蛋白质的肽质量指纹图谱，导致HET-s一级结构覆盖率达87％。获得了HET-s的淀粉样聚集体，并监测了HET-s的可溶性和淀粉样形式的H / D交换。这项研究表明，在HET-s的可溶形式中，C末端区域（从残基240-289跨越）显示出较高的溶剂可及性。形成鲜明对比的是，在该区域中淀粉样蛋白形式的溶剂可及性大大降低。蛋白质（残基1-220）N末端部分的H / D交换速率和水平在可溶和聚集状态下可比。这些结果表明，HET-s的淀粉样蛋白聚集涉及蛋白质的C-末端部分从主要无序到聚集状态的构象转变，其中该区域被高度保护免受氢交换。

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