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首页> 外文期刊>The Journal of biological chemistry >Functional Identification of Toxin-Antitoxin Molecules from Helicobacter pylori 26695 and Structural Elucidation of the Molecular Interactions
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Functional Identification of Toxin-Antitoxin Molecules from Helicobacter pylori 26695 and Structural Elucidation of the Molecular Interactions

机译：来自幽门螺杆菌26695的毒素 - 抗毒素分子的功能鉴定及分子相互作用的结构阐明

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Bacterial toxin-antitoxin (TA) systems are associated with many important cellular processes including antibiotic resistance and microorganism virulence. Here, we identify and structurally characterize TA molecules from the gastric pathogen, Helicobacter pylori. The HP0894 protein had been previously suggested, through our structural genomics approach, to be a putative toxin molecule. In this study, the intrinsic RNase activity and the bacterial cell growth-arresting activity of HP0894 were established. The RNA-binding surface was identified at three residue clusters: (Lys8 and Ser9), (Lys50–Lys54 and Glu58), and (Arg80 and His84–Phe88). In particular, the -UA- and -CA- sequences in RNA were preferentially cleaved by HP0894, and residues Lys52, Trp53, and Ser85–Lys87 were observed to be the main contributors to sequence recognition. The action of HP0894 could be inhibited by the HP0895 protein, and the HP0894-HP0895 complex formed an oligomer with a binding stoichiometry of 1:1. The N and C termini of HP0894 constituted the binding sites to HP0895. In contrast, the unstructured C-terminal region of HP0895 was responsible for binding to HP0894 and underwent a conformational change in the process. Finally, DNA binding activity was observed for both HP0895 and the HP0894-0895 complex but not for HP0894 alone. Taken together, it is concluded that the HP0894-HP0895 protein couple is a TA system in H. pylori, where HP0894 is a toxin with an RNase function, whereas HP0895 is an antitoxin functioning by binding to both the toxin and DNA.
机译：细菌毒素 - 抗毒素（TA）系统与许多重要的细胞方法相关，包括抗生素抗性和微生物毒力。在这里，我们识别和结构地表征来自胃病原体，幽门螺杆菌的TA分子。先前通过我们的结构基因组学方法提出了HP0894蛋白，是推定的毒素分子。在该研究中，建立了内在的RNase活性和HP0894的细菌细胞生长抑制活性。在三个残留物簇中鉴定RNA结合表面：（Lys8和Ser9），（Lys50-Lys54和Glu58），和（Arg80和His84-PHE88）。特别地，通过HP0894优先切割RNA中的-UA和-CA-序列，并且将残留物Lys52，TRP53和Ser85-Lys87观察到序列识别的主要贡献者。 HP0895蛋白质可以抑制HP0894的作用，HP0894-HP0895复合物形成具有1：1的结合化学计量的低聚物。 HP0894的N和C Termini构成了HP0895的结合位点。相反，HP0895的非结构化C末端区域负责结合HP0894，并在该过程中进行了构象变化。最后，对于HP0895和HP0894-0895的复合物，而不是单独的HP0894，观察到DNA结合活性。总之，它得出结论，HP0894-HP0895蛋白夫妇是幽门螺杆菌中的TA系统，其中HP0894是具有RNase功能的毒素，而HP0895是通过与毒素和DNA结合的抗毒素作用。

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