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Host stimuli and operator binding sites controlling protein interactions between virulence master regulator ToxR and ToxS in Vibrio cholerae.
Molecular Microbiology ( IF 2.6 ) Pub Date : 2020-04-06 , DOI: 10.1111/mmi.14510 Mareike Lembke 1 , Thomas Höfler 1 , Ada-Natsuko Walter 1 , Sarah Tutz 1 , Vera Fengler 2 , Stefan Schild 1, 3, 4 , Joachim Reidl 1, 3, 4
Molecular Microbiology ( IF 2.6 ) Pub Date : 2020-04-06 , DOI: 10.1111/mmi.14510 Mareike Lembke 1 , Thomas Höfler 1 , Ada-Natsuko Walter 1 , Sarah Tutz 1 , Vera Fengler 2 , Stefan Schild 1, 3, 4 , Joachim Reidl 1, 3, 4
Affiliation
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Protein–protein interactions (PPIs) are key mechanisms in the maintenance of biological regulatory networks. Herein, we characterize PPIs within ToxR and its co‐activator, ToxS, to understand the mechanisms of ToxR transcription factor activation. ToxR is a key transcription activator that is supported by ToxS for virulence gene regulation in Vibrio cholerae. ToxR comprises a cytoplasmic DNA‐binding domain that is linked by a transmembrane domain to a periplasmic signal receiver domain containing two cysteine residues. ToxR‐ToxR and ToxR‐ToxS PPIs were detected using an adenylate‐cyclase‐based bacterial two‐hybrid system approach in Escherichia coli. We found that the ToxR‐ToxR PPIs are significantly increased in response to ToxR operators, the co‐activator ToxS and bile salts. We suggest that ToxS and bile salts promote the interaction between ToxR molecules that ultimately results in dimerization. Upon binding of operators, ToxR‐ToxR PPIs are found at the highest frequency. Moreover, disulfide‐bond‐dependent interaction in the periplasm results in homodimer formation that is promoted by DNA binding. The formation of these homodimers and the associated transcriptional activity of ToxR were strongly dependent on the oxidoreductases DsbA/DsbC. These findings show that protein and non‐protein partners, that either transiently or stably interact with ToxR, fine‐tune ToxR PPIs, and its associated transcriptional activity in changing environments.
中文翻译：
宿主刺激和操作员结合位点控制霍乱弧菌中毒力主调节因子ToxR和ToxS之间的蛋白质相互作用。
蛋白质间相互作用（PPI）是维持生物调节网络的关键机制。在本文中，我们表征了ToxR及其共激活因子ToxS中的PPI，以了解ToxR转录因子激活的机制。ToxR是关键的转录激活因子，ToxS支持霍乱弧菌的毒性基因调控。ToxR包含一个胞质DNA结合结构域，该结构域通过跨膜结构域与包含两个半胱氨酸残基的周质信号受体结构域相连。在大肠杆菌中使用基于腺苷酸环化酶的细菌双杂交系统方法检测到ToxR-ToxR和ToxR-ToxS PPI。我们发现，ToxR-ToxR PPI显着增加，以响应ToxR操作员，辅激活剂ToxS和胆汁盐。我们建议ToxS和胆盐促进ToxR分子之间的相互作用，最终导致二聚化。绑定运算符后，ToxR-ToxR PPI的出现频率最高。此外，周质中依赖二硫键的相互作用会导致同源二聚体形成，并通过DNA结合促进。这些同二聚体的形成和相关的ToxR转录活性强烈依赖于氧化还原酶DsbA / DsbC。这些发现表明，在不断变化的环境中，与ToxR瞬时或稳定相互作用的蛋白质和非蛋白质伴侣，可以微调ToxR PPI及其相关的转录活性。
更新日期：2020-04-06
中文翻译：
宿主刺激和操作员结合位点控制霍乱弧菌中毒力主调节因子ToxR和ToxS之间的蛋白质相互作用。
蛋白质间相互作用（PPI）是维持生物调节网络的关键机制。在本文中，我们表征了ToxR及其共激活因子ToxS中的PPI，以了解ToxR转录因子激活的机制。ToxR是关键的转录激活因子，ToxS支持霍乱弧菌的毒性基因调控。ToxR包含一个胞质DNA结合结构域，该结构域通过跨膜结构域与包含两个半胱氨酸残基的周质信号受体结构域相连。在大肠杆菌中使用基于腺苷酸环化酶的细菌双杂交系统方法检测到ToxR-ToxR和ToxR-ToxS PPI。我们发现，ToxR-ToxR PPI显着增加，以响应ToxR操作员，辅激活剂ToxS和胆汁盐。我们建议ToxS和胆盐促进ToxR分子之间的相互作用，最终导致二聚化。绑定运算符后，ToxR-ToxR PPI的出现频率最高。此外，周质中依赖二硫键的相互作用会导致同源二聚体形成，并通过DNA结合促进。这些同二聚体的形成和相关的ToxR转录活性强烈依赖于氧化还原酶DsbA / DsbC。这些发现表明，在不断变化的环境中，与ToxR瞬时或稳定相互作用的蛋白质和非蛋白质伴侣，可以微调ToxR PPI及其相关的转录活性。
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