Role of a highly conserved bacterial protein in outer membrane protein assembly
Role of a highly conserved bacterial protein in outer membrane protein assembly
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DOI：
10.1126/science.1078973
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发表时间：
2003-01-10
期刊：
影响因子：
56.9
通讯作者：
Tommassen, J
中科院分区：
文献类型：
--
作者：
Voulhoux, R;Bos, MP;Tommassen, J
在穿过细胞质膜运输后，细菌外膜蛋白被组装到外膜中。脑膜炎球菌Omp85是革兰氏阴性菌中高度保守的蛋白质，其同源物Toc75是叶绿体蛋白质输入机制的组成部分。Omp85似乎是必不可少的活力，和未组装形式的各种外膜蛋白积累Omp85耗尽。免疫荧光显微镜显示减少外膜蛋白的表面暴露，这是特别明显的细胞分裂平面。因此，Omp85可能在外膜蛋白组装中发挥作用。
After transport across the cytoplasmic membrane, bacterial outer membrane proteins are assembled into the outer membrane. Meningococcal Omp85 is a highly conserved protein in Gram-negative bacteria, and its homolog Toc75 is a component of the chloroplast protein-import machinery. Omp85 appeared to be essential for viability, and unassembled forms of various outer membrane proteins accumulated upon Omp85 depletion. Immuno fluorescence microscopy revealed decreased surface exposure of outer membrane proteins, which was particularly apparent at the cell-division planes. Thus, Omp85 is likely to play a role in outer membrane protein assembly.