The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on plV(f1) function
The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on plV(f1) function
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DOI：
10.1046/j.1365-2958.1997.3531727.x
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发表时间：
1997-05-01
影响因子：
3.6
通讯作者：
Russel, M
中科院分区：
文献类型：
--
作者：
Daefler, S;Guilvout, I;Russel, M
相关的外膜蛋白，称为分泌素，参与许多革兰氏阴性菌外膜大分子的分泌。在普鲁兰酶分泌系统中，PulS，一种外膜相关脂蛋白，是保证其分泌素的完整性和外膜定位所必需的。我们发现puls结合位点位于PulD的c端65个残基内。将该结构域添加到丝状噬菌体分泌素plV或不相关的麦芽糖结合蛋白中，使这两种蛋白都依赖PulS来维持稳定性。由噬菌体plV和PulD的c端结构域组成的嵌合蛋白需要适当定位的PuIS来支持噬菌体组装。通过共免疫沉淀和亲和层析检测plV-PulD（65）嵌合体与PulS之间形成的体内复合物。
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, plV, or to the unrelated maltose-binding protein rendered both proteins dependent on PulS for stability. A chimeric protein composed of bacteriophage f1 plV and the C-terminal domain of PulD required properly localized PuIS to support phage assembly. An in vivo complex formed between the plV-PulD(65) chimera and PulS was detected by co-immunoprecipitation and by affinity chromatography.