PROTEIN-D1 - A GLUCOSE-INDUCIBLE, PORE-FORMING PROTEIN FROM THE OUTER-MEMBRANE OF PSEUDOMONAS-AERUGINOSA
PROTEIN-D1 - A GLUCOSE-INDUCIBLE, PORE-FORMING PROTEIN FROM THE OUTER-MEMBRANE OF PSEUDOMONAS-AERUGINOSA
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DOI：
10.1111/j.1574-6968.1980.tb05060.x
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发表时间：
1980-01-01
影响因子：
2.1
通讯作者：
CAREY, AM
中科院分区：
文献类型：
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作者：
HANCOCK, REW;CAREY, AM
铜绿假单胞菌对葡萄糖的摄取可能涉及两种不同的诱导途径，对葡萄糖具有不同的亲和力。葡萄糖Km值为8 vM的高亲和力（低Kin）系统由葡萄糖生长诱导，但不受葡萄糖酸盐、甘油、琥珀酸盐或柠檬酸盐生长诱导[1，2]。Stinson等人[3，4]描述了在相同的生长培养基中诱导的周质葡萄糖结合蛋白，表明该蛋白参与高亲和力系统。此外，已经描述了低亲和力（Km = 1 - 2 mM）葡萄糖转运系统，该系统通过葡萄糖、葡萄糖酸盐和甘油诱导生长，但受到琥珀酸盐和柠檬酸盐的抑制[1，2]。最近，Mizuno和Kageyama [5]描述了在葡萄糖存在下生长的细胞中显著增强的外膜蛋白D。我们证明蛋白D实际上是两种多肽，其中一种蛋白D1仅在细胞在葡萄糖上生长后出现[6]。在本文中，我们证明，蛋白D1诱导生长条件下，导致诱导的高亲和力葡萄糖摄取系统和周质葡萄糖结合蛋白。此外，蛋白质D1已被纯化，并显示重建蔗糖葡萄糖渗透孔的LPS-磷脂囊泡。我们假设该蛋白质是一个外膜葡萄糖孔，类似于
The uptake of glucose by Pseudomonas aeruginosa probably involves two distinct inducible pathways with differing affinities for glucose. A high afffmity (low Kin) system with a K m value of 8 vM for glucose, is induced by growth on glucose but not by growth on gluconate, glycerol, succinate or citrate [1, 2]. Stinson et al.[3, 4] have described a periplasmic glucose binding protein which is induced in the same growth media, suggesting the involvement of this protein in the high affinity system. In addition, a low affinity (K m= 1-2 mM) glucose transport system has been described and is induced by growth on glucose, gluconate and glycerol but is repressed by succinate and citrate [1, 2]. Recently, Mizuno and Kageyama [5] described an outer membrane protein D which was considerably enhanced in cells grown in the presence of glucose. We demonstrated that protein D was in fact two polypeptides, one of which, protein D1, only appeared after growth of cells on glucose [6]. In this paper, we demonstrate that protein D1 is induced under growth conditions which result in induction of the high affinity glucose uptake system and the periplasmic glucose binding protein. Furthermore, protein D1 has been purified and shown to reconstitute sucrose glucose permeable pores in LPS-phospholipid vesicles. We postulate that the protein is an outer membrane glucose pore analogous to the lamB maltose pore of