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首页> 外文期刊>Journal of bacteriology >The N Terminus of FliM Is Essential To Promote Flagellar Rotation in Rhodobacter sphaeroides
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The N Terminus of FliM Is Essential To Promote Flagellar Rotation in Rhodobacter sphaeroides

机译：FliM的N末端对于促进球形红球菌鞭毛旋转至关重要

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摘要

FliM is part of the flagellar switch complex. Interaction of this protein with phospho-CheY (CheY-P) through its N terminus constitutes the main information relay point between the chemotactic system and the flagellum. In this work, we evaluated the role of the N terminus of FliM in the swimming behavior of Rhodobacter sphaeroides. Strains expressing the FliM protein with substitutions in residues previously reported in Escherichia coli as being important for interaction with CheY showed an increased stop frequency compared with wild-type cells. In accordance, we observed that R. sphaeroides cells expressing FliM lacking either the first 13 or 20 amino acids from the N terminus showed a stopped phenotype. We show evidence that FliMΔ13 and FliMΔ20 are stable proteins and that cells expressing them allow flagellin export at levels indistinguishable from those detected for the wild-type strain. These results suggest that the N-terminal region of FliM is required to promote swimming in this bacterium. The role of CheY in controlling flagellar rotation in this organism is discussed.
机译：FliM是鞭毛开关复合体的一部分。该蛋白质通过其N末端与磷酸CheY（CheY-P）的相互作用构成了趋化系统与鞭毛之间的主要信息传递点。在这项工作中，我们评估了FliM的N末端在球形芽孢杆菌的游泳行为中的作用。与野生型细胞相比，以前在大肠杆菌中报道的对与CheY相互作用至关重要的残基中表达FliM蛋白的菌株具有取代作用。据此，我们观察到了 R。表达FliM的Sphaeroides 细胞缺少来自N末端的前13或20个氨基酸，表现出终止的表型。我们显示的证据表明，FliMΔ13和FliMΔ20是稳定的蛋白质，表达它们的细胞允许鞭毛蛋白以与野生型菌株检测到的水平难以区分的水平输出鞭毛蛋白。这些结果表明，需要FliM的N末端区域来促进在该细菌中游泳。讨论了CheY在控制该生物鞭毛旋转中的作用。

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