Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Barcelona, Spain.
PLoS One. 2010 Feb 25;5(2):e9383. doi: 10.1371/journal.pone.0009383.
Protein misfolding is usually deleterious for the cell, either as a consequence of the loss of protein function or the buildup of insoluble and toxic aggregates. The aggregation behavior of a given polypeptide is strongly influenced by the intrinsic properties encoded in its sequence. This has allowed the development of effective computational methods to predict protein aggregation propensity.
METHODOLOGY/PRINCIPAL FINDINGS: Here, we use the AGGRESCAN algorithm to approximate the aggregation profile of an experimental cytosolic Escherichia coli proteome. The analysis indicates that the aggregation propensity of bacterial proteins is associated with their length, conformation, location, function, and abundance. The data are consistent with the predictions of other algorithms on different theoretical proteomes.
CONCLUSIONS/SIGNIFICANCE: Overall, the study suggests that the avoidance of protein aggregation in functional environments acts as a strong evolutionary constraint on polypeptide sequences in both prokaryotic and eukaryotic organisms.
蛋白质错误折叠通常对细胞有害，要么是由于蛋白质功能丧失，要么是由于不溶性和有毒聚集体的积累。给定多肽的聚集行为受到其序列中编码的固有特性的强烈影响。这使得开发有效的计算方法来预测蛋白质聚集倾向成为可能。
方法/主要发现：在这里，我们使用 AGGRESCAN 算法来近似实验胞质大肠杆菌蛋白质组的聚集曲线。分析表明，细菌蛋白的聚集倾向与其长度、构象、位置、功能和丰度有关。这些数据与其他算法在不同理论蛋白质组上的预测一致。
结论/意义：总的来说，这项研究表明，在功能环境中避免蛋白质聚集，对原核和真核生物的多肽序列是一种强大的进化约束。
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