Activation of Histidine Kinase SpaK Is Mediated by the N-Terminal Portion of Subtilin-Like Lantibiotics and Is Independent of Lipid II

Activation of Histidine Kinase SpaK Is Mediated by the N-Terminal Portion of Subtilin-Like Lantibiotics and Is Independent of Lipid II
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组氨酸激酶 SpaK 的激活由枯草菌素样羊毛硫抗生素的 N 末端部分介导,且不依赖于脂质 II

DOI:
10.1128/aem.01368-15
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发表时间:
2015
影响因子:
4.4
通讯作者:
K. Entian
K. Entian
中科院分区:
生物学2区
文献类型:
--
作者:
T. Spieß;S. Korn;P. Kötter;K. Entian

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摘要抗生素枯草杆菌的生物合成是通过组氨酸激酶SPAK在群体感应机制中自动诱导的。枯草杆菌素样抗生素,如瘦肉精、芥菜素S和枯草杆菌素,以类似的方式特异性地激活Spak,而结构相似的Nisin在无毒浓度下不提供Spak激活的信号。然而,令人惊讶的是,如果Nisin与全反式联用,则可部分抑制Spak的激活。N-末端熊果素1-20片段(包括N-末端氨基酸1-20)足以激活Spak,但需要更高的浓度。N端Nisin1-20片段也干扰了醇溶蛋白介导的Spak的激活,并且值得注意的是,在极高的浓度下也激活了Spak。我们的数据表明,N-末端的Entianin1-20片段足以激活Spak。然而,如果存在,分子的C末端部分可能通过干扰细胞膜而进一步强烈地增强激活。通过使用脂类II干扰物质和脂类II缺失突变株的研究表明,脂类II不是传感机制所必需的。
ABSTRACT The biosynthesis of the lantibiotic subtilin is autoinduced in a quorum-sensing mechanism via histidine kinase SpaK. Subtilin-like lantibiotics, such as entianin, ericin S, and subtilin, specifically activated SpaK in a comparable manner, whereas the structurally similar nisin did not provide the signal for SpaK activation at nontoxic concentrations. Surprisingly, nevertheless, nisin if applied together with entianin partly quenched SpaK activation. The N-terminal entianin1–20 fragment (comprising N-terminal amino acids 1 to 20) was sufficient for SpaK activation, although higher concentrations were needed. The N-terminal nisin1–20 fragment also interfered with entianin-mediated activation of SpaK and, remarkably, at extremely high concentrations also activated SpaK. Our data show that the N-terminal entianin1–20 fragment is sufficient for SpaK activation. However, if present, the C-terminal part of the molecule further strongly enhances the activation, possibly by its interference with the cellular membrane. As shown by using lipid II-interfering substances and a lipid II-deficient mutant strain, lipid II is not needed for the sensing mechanism.
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