Barz C, Abahji T N, Trülzsch K, Heesemann J
Max von Pettenkofer-Institut für Hygiene und Medizinische Mikrobiologie, Pettenkoferstrasse 9a, 80336 Munich, Germany.
FEBS Lett. 2000 Sep 29;482(1-2):139-43. doi: 10.1016/s0014-5793(00)02045-7.
Pathogenic bacteria of the genus Yersinia counteract host defense by interfering with eukaryotic signal transduction pathways. YpkA of Yersinia pseudotuberculosis shares significant homology with eukaryotic Ser/Thr protein kinases, is translocated into the host cell and has been shown to be an essential virulence factor in a mouse infection model. In this study, we identify the small GTPases RhoA and Rac-1 as eukaryotic binding partners of YpkA and its homolog YopO of Yersinia enterocolitica. We demonstrate that the interaction is independent of phosphorylation of YpkA and nucleotide loading state of the GTPases. The interaction with RhoA and Rac-1 might provide an important clue to how YpkA interferes with eukaryotic signaling on a molecular level.
耶尔森氏菌属的致病细菌通过干扰真核信号转导途径来对抗宿主防御。假结核耶尔森氏菌的YpkA与真核丝氨酸/苏氨酸蛋白激酶具有显著同源性,可转运至宿主细胞内,并且在小鼠感染模型中已被证明是一种必需的毒力因子。在本研究中,我们鉴定出小GTP酶RhoA和Rac-1是YpkA及其小肠结肠炎耶尔森氏菌同源物YopO的真核结合伴侣。我们证明这种相互作用独立于YpkA的磷酸化和GTP酶的核苷酸负载状态。与RhoA和Rac-1的相互作用可能为YpkA如何在分子水平上干扰真核信号传导提供重要线索。