A role for the essential YycG sensor histidine kinase in sensing cell division.
A role for the essential YycG sensor histidine kinase in sensing cell division.
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DOI：
10.1111/j.1365-2958.2010.07464.x
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发表时间：
2011-01
影响因子：
3.6
通讯作者：
Szurmant H
中科院分区：
文献类型：
--
作者：
Fukushima T;Furihata I;Emmins R;Daniel RA;Hoch JA;Szurmant H
YycG（WalK）传感器组氨酸激酶通过控制自溶素及其抑制剂的基因转录来协调革兰氏阳性细菌中的细胞壁重塑与细胞分裂。枯草芽孢杆菌YycG感测细胞分裂，并通过与分裂隔膜处的分裂体结合而被酶促激活。在这里，它表明，这种多结构域跨膜激酶的细胞质PAS结构域是一个决定因素的激酶易位到分裂隔膜。此外，易位到分裂隔膜，本身，是不足以激活YycG，这表明，特定的相互作用和/或产生的配体需要刺激激酶活性。YycG的N-末端截短失去其活性的负调控，推断这种调控是通过其跨膜和膜外结构域与膜相关的YycH和YycI蛋白相互作用而完成的，所述蛋白不定位于分裂体。这些数据表明，YycG活性在非分裂细胞中受到抑制，其与YycH和YycI的相互作用，其激活是协调分裂细胞中的细胞分裂，通过特定的相互作用，发生在分裂体内。
The YycG (WalK) sensor histidine kinase coordinates cell wall remodeling with cell division in Gram-positive bacteria by controlling the transcription of genes for autolysins and their inhibitors. Bacillus subtilis YycG senses cell division and is enzymatically activated by associating with the divisome at the division septum. Here it is shown that the cytoplasmic PAS domain of this multi-domain trans-membrane kinase is a determining factor translocating the kinase to the division septum. Furthermore, translocation to the division septum, per se, is insufficient to activate YycG, indicating that specific interactions and/or ligands produced there are required to stimulate kinase activity. N-terminal truncations of YycG lose negative regulation of their activity inferring that this regulation is accomplished through its transmembrane and extra-membrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome. The data indicate that YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI and its activation is coordinated to cell division in dividing cells by specific interactions that occur within the divisome.
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