Daefler S, Guilvout I, Hardie K R, Pugsley A P, Russel M
Rockefeller University, New York, New York 10021, USA.
Mol Microbiol. 1997 May;24(3):465-75. doi: 10.1046/j.1365-2958.1997.3531727.x.
Related outer membrane proteins, termed secretins, participate in the secretion of macromolecules across the outer membrane of many Gram-negative bacteria. In the pullulanase-secretion system, PulS, an outer membrane-associated lipoprotein, is required both for the integrity and the proper outer membrane localization of the PulD secretin. Here we show that the PulS-binding site is located within the C-terminal 65 residues of PulD. Addition of this domain to the filamentous phage secretin, pIV, or to the unrelated maltose-binding protein rendered both proteins dependent on PulS for stability. A chimeric protein composed of bacteriophage f1 pIV and the C-terminal domain of PuID required properly localized PulS to support phage assembly. An in vivo complex formed between the pIV-PulD65 chimera and PulS was detected by co-immunoprecipitation and by affinity chromatography.
相关的外膜蛋白，即分泌素，参与许多革兰氏阴性菌外膜大分子的分泌。在支链淀粉酶分泌系统中，PulS是一种与外膜相关的脂蛋白，对于PulD分泌素的完整性和正确的外膜定位都是必需的。我们在此表明，PulS结合位点位于PulD的C末端65个残基内。将该结构域添加到丝状噬菌体分泌素pIV或不相关的麦芽糖结合蛋白上，会使这两种蛋白的稳定性都依赖于PulS。由噬菌体f1 pIV和PulD的C末端结构域组成的嵌合蛋白需要正确定位的PulS来支持噬菌体组装。通过共免疫沉淀和亲和层析检测到pIV-PulD65嵌合体与PulS之间在体内形成的复合物。
