Prinz T, Tommassen J
Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
FEMS Microbiol Lett. 2000 Feb 1;183(1):49-53. doi: 10.1111/j.1574-6968.2000.tb08932.x.
The RmpM (class 4) protein of Neisseria meningitidis has previously been shown to be associated with the outer membrane porins. In the present study, we demonstrate that this protein forms complexes with the lactoferrin receptor LbpA, the transferrin receptor TbpA and the siderophore receptor FrpB as well. This complexation apparently resulted in a stabilization of oligomeric forms of these iron-regulated proteins. In vitro experiments further revealed a reduced ability to acquire iron from human lactoferrin in the rmpM mutant. Furthermore, all TonB-dependent receptors investigated here appeared to exist as oligomers (probably dimers), suggesting that this is a general feature of this class of proteins.
脑膜炎奈瑟菌的RmpM(4类)蛋白先前已被证明与外膜孔蛋白相关。在本研究中,我们证明该蛋白还与乳铁蛋白受体LbpA、转铁蛋白受体TbpA和铁载体受体FrpB形成复合物。这种复合显然导致了这些铁调节蛋白寡聚体形式的稳定。体外实验进一步揭示,rmpM突变体从人乳铁蛋白获取铁的能力降低。此外,这里研究的所有TonB依赖性受体似乎都以寡聚体(可能是二聚体)形式存在,这表明这是这类蛋白的一个普遍特征。