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首页> 外文期刊>Cell biology international. >The composition of the polyglutamine-containing proteins influences their co-aggregation properties.
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The composition of the polyglutamine-containing proteins influences their co-aggregation properties.

机译：含聚谷氨酰胺的蛋白质的组成会影响其共聚集特性。

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摘要

The sequestration of crucial cellular proteins into insoluble aggregates formed by the polypeptides containing expanded polyglutamine tracts has been proposed to be the key mechanism responsible for the abnormal cell functioning in the so-called polyglutamine diseases. To evaluate to what extent the ability of polyglutamine sequences to recruit other proteins into the intracellular aggregates depends on the composition of the aggregating peptide, we analysed the co-aggregation properties of the N-terminal fragment of huntingtin fused with unrelated non-aggregating and/or self-aggregating peptides. We show that the ability of the mutated N-terminal huntingtin fragment to sequester non-related proteins can be significantly increased by fusion with the non-aggregating reporter protein [GFP (green fluorescence protein)]. By contrast, fusion with the self-aggregating C-terminal fragment of the CFTR (cystic fibrosis transmembrane conductance regulator) dramatically reduces the sequestration of related non-fused huntingtin fragments. We also demonstrate that the co-aggregation of different non-fused N-terminal huntingtin fragments depends on their length, with long fragments of the wild-type huntingtin not only excluded from the nuclear inclusions, but also very inefficiently sequestered into the cytoplasmic aggregates formed by the short fragments of mutant protein. Additionally, our results suggest that atypical intracellular aggregation patterns, which include unusual distribution and/or morphology of protein aggregates, are associated with altered ability of accumulating proteins to co-aggregate with other peptides.
机译：已提出将关键的细胞蛋白螯合成由含有扩展的聚谷氨酰胺束的多肽形成的不溶性聚集体，是造成所谓的聚谷氨酰胺疾病中异常细胞功能的关键机制。为了评估聚谷氨酰胺序列将其他蛋白质募集到细胞内聚集体的能力在多大程度上取决于聚集肽的组成，我们分析了亨廷顿蛋白N末端片段与无关的非聚集和/或融合的共聚集特性。或自聚集肽。我们显示突变的N末端亨廷顿蛋白片段隔离非相关蛋白的能力可以通过与非聚集报道蛋白[GFP（绿色荧光蛋白）]融合而显着增加。相比之下，与CFTR（囊性纤维化跨膜电导调节剂）的自聚集C端片段的融合显着减少了相关非融合亨廷顿蛋白片段的螯合。我们还证明了不同的非融合N末端亨廷顿蛋白片段的共聚集取决于它们的长度，野生型亨廷顿蛋白的长片段不仅被排除在核内含物中，而且还非常低效地被隔离成形成的胞质聚集体由突变蛋白的短片段组成。此外，我们的结果表明，非典型的细胞内聚集模式（包括蛋白质聚集体的异常分布和/或形态）与积累蛋白质与其他肽共聚集的能力发生了变化。

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