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首页> 美国卫生研究院文献>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：幽门螺杆菌26695毒素-抗毒素分子的功能鉴定和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过程相关，包括抗生素抗性和微生物毒力。在这里，我们从胃病原体幽门螺杆菌中鉴定和分子表征TA分子。通过我们的结构基因组学方法，HP0894蛋白先前被认为是推定的毒素分子。在这项研究中，建立了固有的RNase活性和HP0894的细菌细胞阻滞活性。在三个残基簇上鉴定了RNA结合表面：（Lys 8 和Ser 9 ），（Lys 50 –Lys 54 和Glu 58 ），以及（Arg 80 和His 84 –Phe 88 ）。特别是，HP0894优先切割RNA中的-UA-和-CA-序列，残基为Lys 52 ，Trp 53 和Ser 85 –Lys 87 被认为是序列识别的主要贡献者。 HP0895蛋白可抑制HP0894的作用，而HP0894-HP0895络合物形成结合化学计量比为1：1的低聚物。 HP0894的N和C末端构成与HP0895的结合位点。相反，HP0895的非结构化C末端区域负责与HP0894结合，并在此过程中发生构象变化。最后，对HP0895和HP0894-0895复合体均观察到了DNA结合活性，但对单独的HP0894没有观察到。两者合计，可以得出结论，HP0894-HP0895蛋白对是幽门螺杆菌中的TA系统，其中HP0894是具有RNase功能的毒素，而HP0895是通过结合毒素和DNA起作用的抗毒素。

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