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首页> 外文期刊>BMC Microbiology >Identification of Archaea-specific chemotaxis proteins which interact with the flagellar apparatus
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Identification of Archaea-specific chemotaxis proteins which interact with the flagellar apparatus

机译：鉴定与鞭毛器相互作用的古细菌特异性趋化蛋白

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Background Archaea share with bacteria the ability to bias their movement towards more favorable locations, a process known as taxis. Two molecular systems drive this process: the motility apparatus and the chemotaxis signal transduction system. The first consists of the flagellum, the flagellar motor, and its switch, which allows cells to reverse the rotation of flagella. The second targets the flagellar motor switch in order to modulate the switching frequency in response to external stimuli. While the signal transduction system is conserved throughout archaea and bacteria, the archaeal flagellar apparatus is different from the bacterial one. The proteins constituting the flagellar motor and its switch in archaea have not yet been identified, and the connection between the bacterial-like chemotaxis signal transduction system and the archaeal motility apparatus is unknown. Results Using protein-protein interaction analysis, we have identified three proteins in Halobacterium salinarum that interact with the chemotaxis (Che) proteins CheY, CheD, and CheC2, as well as the flagella accessory (Fla) proteins FlaCE and FlaD. Two of the proteins belong to the protein family DUF439, the third is a HEAT_PBS family protein. In-frame deletion strains for all three proteins were generated and analyzed as follows: a) photophobic responses were measured by a computer-based cell tracking system b) flagellar rotational bias was determined by dark-field microscopy, and c) chemotactic behavior was analyzed by a swarm plate assay. Strains deleted for the HEAT_PBS protein or one of the DUF439 proteins proved unable to switch the direction of flagellar rotation. In these mutants, flagella rotate only clockwise, resulting in exclusively forward swimming cells that are unable to respond to tactic signals. Deletion of the second DUF439 protein had only minimal effects. HEAT_PBS proteins could be identified in the chemotaxis gene regions of all motile haloarchaea sequenced so far, but not in those of other archaeal species. Genes coding for DUF439 proteins, however, were found to be integral parts of chemotaxis gene regions across the archaeal domain, and they were not detected in other genomic context. Conclusion Altogether, these results demonstrate that, in the archaeal domain, previously unrecognized archaea-specific Che proteins are essential for relaying taxis signaling to the flagellar apparatus.
机译：背景古细菌与细菌共享将其运动偏向更有利位置的能力，这一过程称为出租车。有两个分子系统驱动这一过程：运动设备和趋化信号转导系统。第一个由鞭毛，鞭毛马达及其开关组成，允许细胞逆转鞭毛的旋转。第二个目标是鞭毛电动机开关，以便响应外部刺激来调节开关频率。尽管信号转导系统在整个古细菌和细菌中都得到保护，但古细菌的鞭毛器不同于细菌的鞭毛器。尚未发现构成鞭毛马达及其在古细菌中的开关的蛋白质，细菌样趋化信号转导系统与古细菌运动装置之间的联系尚不清楚。结果使用蛋白质-蛋白质相互作用分析，我们在盐杆菌中鉴定了三种与趋化性（Che）蛋白质CheY，CheD和CheC2相互作用的鞭毛，以及鞭毛辅助（Fla）蛋白质FlaCE和FlaD。其中两个蛋白属于DUF439蛋白家族，第三个蛋白是HEAT_PBS家族蛋白。生成并分析了所有三种蛋白质的框内缺失菌株：a）通过基于计算机的细胞跟踪系统测量畏光反应b）通过暗视野显微镜确定鞭毛旋转偏斜，并c）分析趋化行为通过群体平板分析。事实证明，缺失了HEAT_PBS蛋白或DUF439蛋白之一的菌株无法改变鞭毛旋转的方向。在这些突变体中，鞭毛仅顺时针旋转，从而导致无法响应战术信号的前向游泳细胞。删除第二个DUF439蛋白的作用很小。 HEAT_PBS蛋白可以在到目前为止已测序的所有运动型盐生古细菌的趋化性基因区域中找到，但在其他古生菌物种中却没有。但是，发现编码DUF439蛋白的基因是整个古细菌域趋化性基因区域的组成部分，在其他基因组环境中未检测到。结论总而言之，这些结果表明，在古细菌域中，以前无法识别的古细菌特异性Che蛋白对于将滑行信号转导至鞭毛器至关重要。

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