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Structural insights into the inhibition mechanism of bacterial toxin LsoA by bacteriophage antitoxin Dmd
Wan H(万华); Wan, H; Gao ZQ(高增强); Otsuka, Y; Gao, ZQ; Wei, Y; Chen, Z; Masuda, M; Yonesaki, T; Zhang, H; Dong, YH; Wei Y(魏勇); Chen Z(陈真); Zhang H(张衡); Dong YH(董宇辉)
2016
发表期刊MOLECULAR MICROBIOLOGY
卷号101期号:5页码:757-769
通讯作者董宇辉
文章类型期刊论文
摘要Bacteria have obtained a variety of resistance mechanisms including toxin-antitoxin (TA) systems against bacteriophages (phages), whereas phages have also evolved to overcome bacterial anti-phage mechanisms. Dmd from T4 phage can suppress the toxicities of homologous toxins LsoA and RnlA from Escherichia coli, representing the first example of a phage antitoxin against multiple bacterial toxins in known TA systems. Here, the crystal structure of LsoA-Dmd complex showed Dmd is inserted into the deep groove between the N-terminal repeated domain (NRD) and the Dmd-binding domain (DBD) of LsoA. The NRD shifts significantly from a 'closed' to an 'open' conformation upon Dmd binding. Site-directed mutagenesis of Dmd revealed the conserved residues (W31 and N40) are necessary for LsoA binding and the toxicity suppression as determined by pull-down and cell toxicity assays. Further mutagenesis identified the conserved Dmd-binding residues (R243, E246 and R305) of LsoA are vital for its toxicity, and suggested Dmd and LsoB may possess different inhibitory mechanisms against LsoA toxicity. Our structure-function studies demonstrate Dmd can recognize LsoA and inhibit its toxicity by occupying the active site possibly via substrate mimicry. These findings have provided unique insights into the defense and counter-defense mechanisms between bacteria and phages in their co-evolution.
DOI10.1111/mmi.13420
关键词[WOS]ESCHERICHIA-COLI TOXIN ; ABORTIVE INFECTION SYSTEM ; RNASE LS ; PHAGE ; RNLA ; RESISTANCE ; SOFTWARE ; FEATURES ; MAZF
语种英语
WOS类目Biochemistry & Molecular Biology ; Microbiology
WOS记录号WOS:000384410300005
引用统计
被引频次:2[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/260467
专题多学科研究中心
作者单位中国科学院高能物理研究所
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GB/T 7714
Wan H,Wan, H,Gao ZQ,et al. Structural insights into the inhibition mechanism of bacterial toxin LsoA by bacteriophage antitoxin Dmd[J]. MOLECULAR MICROBIOLOGY,2016,101(5):757-769.
APA 万华.,Wan, H.,高增强.,Otsuka, Y.,Gao, ZQ.,...&董宇辉.(2016).Structural insights into the inhibition mechanism of bacterial toxin LsoA by bacteriophage antitoxin Dmd.MOLECULAR MICROBIOLOGY,101(5),757-769.
MLA 万华,et al."Structural insights into the inhibition mechanism of bacterial toxin LsoA by bacteriophage antitoxin Dmd".MOLECULAR MICROBIOLOGY 101.5(2016):757-769.
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