Signal binding at both modules of its dCache domain enables the McpA chemoreceptor of Bacillus velezensis to sense different ligands.

Signal binding at both modules of its dCache domain enables the McpA chemoreceptor of Bacillus velezensis to sense different ligands.
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dCache 域两个模块上的信号结合使贝莱森芽孢杆菌的 McpA 化学感受器能够感知不同的配体

DOI:
10.1073/pnas.2201747119
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发表时间:
2022-07-19
影响因子:
11.1
通讯作者:
Zhang, Ruifu
Zhang, Ruifu
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Feng, Haichao;Lv, Yu;Krell, Tino;Fu, Ruixin;Liu, Yunpeng;Xu, Zhihui;Du, Wenbin;Shen, Qirong;Zhang, Nan;Zhang, Ruifu

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dCache显示出普遍存在的系统发育分布,并且大量存在于古细菌、细菌和真核生物中。它是主要的细菌胞外传感器结构域,存在于所有主要的跨膜受体家族中。大多数表征的dCache介导对二硫键类似配体的反应,发现其与膜远端模块结合。虽然也有证据表明其他dCache对多个配体有反应,但目前有关相应分子机制的信息有限。我们在这里表明,响应多个配体的能力是由于利用两个dCache模块。这项工作提供了有关导致dCache结构域演变的力量的信息,并提供了表征具有窄和宽配体范围的受体的特征。细菌已经进化出多种信号转导系统,使其能够适应不断变化的环境条件。基于化学受体的信号级联在细菌中非常丰富,并且是最复杂的信号系统之一。目前,我们对化学感受器信号识别的分子特征的了解有限。已显示Velezensis SQR9的化学受体McpA介导对宽范围的不同配体的趋化性。在这里,我们表明,其配体结合域直接结合13化学引诱物。我们提供的支持,有机酸和氨基酸结合到膜远端和膜近端模块的dCache域,分别,而糖/糖醇的结合发生在这两个模块。结构生物学研究结合定点诱变实验已经允许鉴定在多种配体的识别中起关键作用的10个氨基酸残基。膜远端和膜近端区域的残基分别是有机酸和氨基酸的敏感中心,而所有残基都参与了糖/糖醇的敏感。大多数特征化的化学受体具有狭窄且明确的配体谱。我们在这里提出了一种涉及两个dCache模块的传感机制,该机制允许通过单个化学感受器整合非常多样化的信号。
The dCache shows a ubiquitous phylogenetic distribution and is abundantly present in archaea, bacteria, and eukaryota. It’s the predominant bacterial extracytosolic sensor domain and present in all major families of transmembrane receptors. Most characterized dCache mediate responses to diversely similar ligands, which were found to bind to the membrane-distal module. Although there’s also evidence that other dCache respond to multiple ligands, the information on the corresponding molecular mechanism is currently limited. We show here that the capacity to respond to multiple ligands is due to the utilization of both dCache modules. This work provides information on the forces that have led to the evolution of dCache domains and provides features that characterize receptors with narrow and broad ligand ranges. Bacteria have evolved multiple signal transduction systems that permit an adaptation to changing environmental conditions. Chemoreceptor-based signaling cascades are very abundant in bacteria and are among the most complex signaling systems. Currently, our knowledge on the molecular features that determine signal recognition at chemoreceptors is limited. Chemoreceptor McpA of Bacillus velezensis SQR9 has been shown to mediate chemotaxis to a broad range of different ligands. Here we show that its ligand binding domain binds directly 13 chemoattractants. We provide support that organic acids and amino acids bind to the membrane-distal and membrane-proximal module of the dCache domain, respectively, whereas binding of sugars/sugar alcohols occurred at both modules. Structural biology studies combined with site-directed mutagenesis experiments have permitted to identify 10 amino acid residues that play key roles in the recognition of multiple ligands. Residues in membrane-distal and membrane-proximal regions were central for sensing organic acids and amimo acids, respectively, whereas all residues participated in sugars/sugar alcohol sensing. Most characterized chemoreceptors possess a narrow and well-defined ligand spectrum. We propose here a sensing mechanism involving both dCache modules that allows the integration of very diverse signals by a single chemoreceptor.
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发表时间: 2018-06-22
影响因子: 5.6
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