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Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias

机译：额颞痴呆的tau突变体的结构，微管相互作用和成对的螺旋丝聚集

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We have studied biochemical and structural parameters of several missense and deletion mutants of tau protein (G272V, N279K, Delta K280, P301L, V337M, R406W) found in frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). The mutant proteins were expressed on the basis of both full-length tau (htau40) and constructs derived from the repeat domain. They were analyzed with respect to the capacity to enhance microtubule assembly, binding of tau to microtubules, secondary structure content, and aggregation into Alzheimer-like paired helical or straight filaments. We find that the mutations cause a moderate decrease in microtubule interactions and stabilization, and they show no gross structural changes compared with the natively unfolded conformation of the wild-type protein, but the aggregation into PHFs is strongly enhanced, particularly for the mutants Delta K280 and P301L. This gain of pathological aggregation would be consistent with the autosomal dominant nature of the disease. [References: 59]
机译：我们研究了额颞叶痴呆和与17号染色​​体（FTDP-17）相关的帕金森病中发现的几种tau蛋白错义和缺失突变体（G272V，N279K，Delta K280，P301L，V337M，R406W）的生化和结构参数。突变蛋白基于全长tau（htau40）和衍生自重复结构域的构建体表达。分析了它们增强微管组装的能力，tau与微管的结合，二级结构含量以及聚集成阿尔茨海默氏样成对的螺旋或直丝的能力。我们发现，突变引起微管相互作用和稳定性的适度降低，并且与野生型蛋白的天然展开构象相比，它们没有显示总体结构变化，但向PHFs的聚集作用得到了显着增强，尤其是对于突变体Delta K280和P301L。这种病理性聚集的获得将与疾病的常染色体显性遗传相一致。 [参考：59]

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