A cell-cell signaling peptide activates the PlcR virulence regulon in bacteria of the Bacillus cereus group
A cell-cell signaling peptide activates the PlcR virulence regulon in bacteria of the Bacillus cereus group
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DOI：
10.1093/emboj/cdf450
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发表时间：
2002-09-02
期刊：
影响因子：
11.4
通讯作者：
Lereclus, D
中科院分区：
文献类型：
--
作者：
Slamti, L;Lereclus, D
PlcR是一种多效性调节因子，可激活苏云金芽孢杆菌和蜡状芽孢杆菌中编码各种毒力因子（如磷脂酶C、蛋白酶和溶血素）的基因的表达。在这里，我们表明，激活机制是在一个小肽的控制下：PapR。papR基因属于PlcR调节子，位于plcR下游70 bp处。它编码一个48个氨基酸的肽。破坏papR基因废除的PlcR调节子的表达，导致在昆虫幼虫的溶血和毒力的大幅度下降。我们证明，PapR多肽分泌，然后通过寡肽通透酶Opp重新进口。一旦在细胞内，加工形式的PapR，大概是一个五肽，激活PlcR调节子，允许PlcR结合到它的DNA目标。发现这种激活机制是菌株特异性的，这种特异性由五肽的第一个残基决定。
PlcR is a pleiotropic regulator that activates the expression of genes encoding various virulence factors, such as phospholipases C, proteases and hemolysins, in Bacillus thuringiensis and Bacillus cereus. Here we show that the activation mechanism is under the control of a small peptide: PapR. The papR gene belongs to the PlcR regulon and is located 70 bp downstream from plcR. It encodes a 48-amino-acid peptide. Disruption of the papR gene abolished expression of the PlcR regulon, resulting in a large decrease in hemolysis and virulence in insect larvae. We demonstrated that the PapR polypeptide was secreted, then reimported via the oligopeptide permease Opp. Once inside the cell, a processed form of PapR, presumably a pentapeptide, activated the PlcR regulon by allowing PlcR to bind to its DNA target. This activating mechanism was found to be strain specific, with this specificity determined by the first residue of the penta peptide.