Sigma factor S (σ^S) are master regulator responsible for the survival of bacteria under extreme conditions. Bacteria start specific gene expression via σ^S promoter recognition, activating various responses to cope with external conditions. Although this self-protection mechanism is vital for bacteria to propagate and evolve, there are many puzzling research questions to be answered. For example, while interactions between σ^S, transcription regulator RssB, and anti-adaptor Ira proteins are believed to be responsible for controlling the cellular level of σ^S, their competition mechanism among them remains elusive. Furthermore, there are still debates on the location of the interface of Ira proteins and RssB and whether phosphorylation on the receiver domain is essential for σ^S activation remains elusive. While there is one crystal structure for the Escherichia coli receiver domain deposited in the database, the missing regions in the structure become an obstacle for functional and interactive studies. Despite attempts, there is no structure for any protein complex in this important biological process, making it one overlooked area in bacterial transcription. Here, using solution-state NMR, our near-complete resonance assignment for the receiver domain of E. coli RssB provides a basis for future structure determination and interaction studies with its many known and putative ligands.

中文翻译：

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大肠杆菌的sigma因子S调节剂RssB的N末端受体域的共振分配。

σ因子S（σ^小号）是主调节器负责细菌的极端条件下存活。细菌开始经由σ特异性基因表达^小号启动子识别，激活各种响应，以应付外部条件。尽管这种自我保护机制对于细菌的繁殖和进化至关重要，但仍有许多令人困惑的研究问题需要解答。例如，虽然σ之间的相互作用^小号，转录调节RSSB和抗适配器艾拉蛋白被认为是负责控制σ的细胞水平^小号，他们之间的竞争机制仍然难以捉摸。此外，仍有争论上艾拉蛋白质和RSSB的界面的位置，以及是否在接收器结构域磷酸化是必不可少σ^小号活化仍然是难以捉摸的。尽管在数据库中存放了大肠杆菌受体结构域的一种晶体结构，但结构中的缺失区域成为功能和相互作用研究的障碍。尽管进行了尝试，但在这一重要的生物学过程中没有任何蛋白质复合物的结构，这使其成为细菌转录中一个被忽视的领域。在这里，使用溶液态NMR，我们对大肠杆菌受体域的接近完全共振分配 RssB为将来的结构确定及其与许多已知的和推定的配体的相互作用研究提供了基础。