Functionally important multidomain bacterial protein bS1 is the largest ribosomal protein of subunit 30S. It interacts with both mRNA and proteins and is prone to aggregation, although this process has not been studied in detail. Here, we obtained bacterial strains overproducing ribosomal bS1 protein from Thermus thermophilus and its stable fragment bS1(49) and purified these proteins. Using fluorescence spectroscopy, dynamic light scattering, and high-performance liquid chromatography combined with mass spectrometric analysis of products of protein limited proteolysis, we demonstrated that disordered regions at the N- and C-termini of bS1 can play a key role in the aggregation of this protein. The truncated fragment bS1(49) was less prone to aggregation compared to the full-size bS1. The revealed properties of the studied proteins can be used to obtain protein crystals for elucidating the structure of the bS1 stable fragment.

中文翻译：

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嗜热栖热菌核糖体蛋白bS1及其稳定片段聚集的比较分析

功能重要的多域细菌蛋白 bS1 是最大的 30S 亚基核糖体蛋白。它与 mRNA 和蛋白质相互作用并易于聚集，尽管尚未详细研究该过程。在这里，我们从嗜热栖热菌及其稳定片段 bS1(49) 中获得了过量生产核糖体 bS1 蛋白的细菌菌株，并纯化了这些蛋白质。使用荧光光谱、动态光散射和高效液相色谱结合蛋白质有限蛋白水解产物的质谱分析，我们证明 bS1 的 N 和 C 末端的无序区域可以在聚合中起关键作用。这种蛋白质。与全尺寸 bS1 相比，截短的 bS1(49) 片段不太容易聚集。