Schmitt Simone, Prokisch Holger, Schlunck Tilman, Camp David G, Ahting Uwe, Waizenegger Thomas, Scharfe Curt, Meitinger Thomas, Imhof Axel, Neupert Walter, Oefner Peter J, Rapaport Doron
Institute for Physiological Chemistry, Ludwig-Maximillians-Universität, Butenandstrasse 5, 81377 Munich, Germany.
Proteomics. 2006 Jan;6(1):72-80. doi: 10.1002/pmic.200402084.
The mitochondrial outer membrane mediates numerous interactions between the metabolic and genetic systems of mitochondria and the rest of the eukaryotic cell. We performed a proteomic study to discover novel functions of components of the mitochondrial outer membrane. Proteins of highly pure outer membrane vesicles (OMV) from Neurospora crassa were identified by a combination of LC-MS/MS of tryptic peptide digests and gel electrophoresis of solubilized OMV proteins, followed by their identification using MALDI-MS PMF. Among the 30 proteins found in at least three of four separate analyses were 23 proteins with known functions in the outer membrane. These included components of the import machinery (the TOM and TOB complexes), a pore-forming component (porin), and proteins that control fusion and fission of the organelle. In addition, proteins playing a role in various biosynthetic pathways, whose intracellular location had not been established previously, could be localized to the mitochondrial outer membrane. Thus, the proteome of the outer membrane can help in identifying new mitochondria-related functions.
线粒体外膜介导了线粒体的代谢和遗传系统与真核细胞其他部分之间的众多相互作用。我们进行了一项蛋白质组学研究，以发现线粒体外膜成分的新功能。通过胰蛋白酶肽段消化产物的液相色谱-串联质谱（LC-MS/MS）和溶解的线粒体外膜囊泡（OMV）蛋白的凝胶电泳相结合的方法，鉴定了来自粗糙脉孢菌的高度纯化的外膜囊泡中的蛋白质，随后使用基质辅助激光解吸电离质谱（MALDI-MS）肽质量指纹图谱（PMF）对其进行鉴定。在四个独立分析中至少三次检测到的30种蛋白质中，有23种蛋白质在外膜中具有已知功能。这些蛋白质包括导入机制的成分（TOM和TOB复合物）、一种成孔成分（孔蛋白）以及控制细胞器融合和裂变的蛋白质。此外，在各种生物合成途径中发挥作用但此前细胞内定位尚未确定的蛋白质，也可定位于线粒体外膜。因此，外膜蛋白质组有助于识别与线粒体相关的新功能。
