MotPS is the stator-force generator for motility of alkaliphilic Bacillus, and its homologue is a second functional Mot in Bacillus subtilis

MotPS is the stator-force generator for motility of alkaliphilic Bacillus, and its homologue is a second functional Mot in Bacillus subtilis
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DOI:
10.1111/j.1365-2958.2004.04173.x
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发表时间:
2004-08-01
影响因子:
3.6
通讯作者:
Krulwich, TA
Krulwich, TA
中科院分区:
生物学2区
文献类型:
--
作者:
Ito, M;Hicks, DB;Krulwich, TA

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在嗜碱假坚强芽孢杆菌OF4中驱动Na+依赖性运动的定子力发生器在此被鉴定为MotPS,MotAB样蛋白,其基因位于ccpA基因的下游,ccpA基因编码碳代谢的主要调节因子。B。pseudofirmus OF4仅在pH值高于8时才能活动。破坏的motPS导致在一个非运动的表型,和运动性恢复与含有motPS基因的多拷贝质粒转化。从B纯化并重构MotPS。pseudofirmus OF 4催化阿米洛利类似物敏感的Na+转运。与B相反。pseudofirmus,枯草芽孢杆菌含有MotAB和MotPS系统。来自B的motPS基因的作用。在具有完整的motAB和motPS基因座、仅两个mot系统中的一个或两个mot系统都没有的等基因菌株中测试了枯草芽孢杆菌在几种基于运动性的行为中的表现。B。枯草杆菌MotPS(BsMotPS)支持Na+刺激的运动性,软琼脂表面上的趋化性和生物膜形成,特别是在选择向上运动的变体后。BsMotPS也支持运动在琼脂软塞浸在液体中,运动被完全抑制阿米洛利类似物。BsMotPS不支持在较高浓度琼脂表面上的表面活性素依赖性群集。这些结果表明,BsMotPS有助于B实验室菌株在软琼脂上的生物膜形成和运动性,但不有助于集群。其中MotAB是占主导地位的定子力发生器。BsMotPS可能是B中运动性的潜在优势。枯草芽孢杆菌变种出现在特定的小生境。
The stator-force generator that drives Na+-dependent motility in alkaliphilic Bacillus pseudofirmus OF4 is identified here as MotPS, MotAB-like proteins with genes that are downstream of the ccpA gene, which encodes a major regulator of carbon metabolism. B. pseudofirmus OF4 was only motile at pH values above 8. Disruption of motPS resulted in a non-motile phenotype, and motility was restored by transformation with a multicopy plasmid containing the motPS genes. Purified and reconstituted MotPS from B. pseudofirmus OF4 catalysed amiloride analogue-sensitive Na+ translocation. In contrast to B. pseudofirmus, Bacillus subtilis contains both MotAB and MotPS systems. The role of the motPS genes from B. subtilis in several motility-based behaviours was tested in isogenic strains with intact motAB and motPS loci, only one of the two mot systems or neither mot system. B. subtilis MotPS (BsMotPS) supported Na+-stimulated motility, chemotaxis on soft agar surfaces and biofilm formation, especially after selection of an up-motile variant. BsMotPS also supported motility in agar soft plugs immersed in liquid; motility was completely inhibited by an amiloride analogue. BsMotPS did not support surfactin-dependent swarming on higher concentration agar surfaces. These results indicate that BsMotPS contributes to biofilm formation and motility on soft agar, but not to swarming, in laboratory strains of B. subtilis in which MotAB is the dominant stator-force generator. BsMotPS could potentially be dominant for motility in B. subtilis variants that arise in particular niches.