Department of Biology, University of Genoa, Viale Bendetto XV, 5, 16132 Genova, Italy.
Expert Rev Proteomics. 2011 Apr;8(2):231-9. doi: 10.1586/epr.11.1.
Expression of F1Fo-ATP synthase, which generates the majority of cellular ATP and is believed to be strictly confined to mitochondria, has recently been identified in ectopic locations, together with the four complexes of oxidative phosphorylation (OXPHOS) or enzymes from the Krebs cycle. Identification of these proteins has mostly been accomplished by proteomic methods and mass spectrometry - techniques that hold great promise in increasing our understanding of the proteome. The ectopic presence of ATP synthase has variably been attributed to contamination of the sample or to its action as a cell-surface receptor for apparently unrelated ligands, but OXPHOS proteins have sometimes been found to be catalytically active in oxidative phosphorylation, as they were true components of the system under investigation. The present article focuses on how mass spectrometry can increase our understanding of the proteome of subcellular membranes. We review the recent evidence for an extra-mitochondrial expression of OXPHOS by proteomics studies, highlighting what we can learn by combining these data.
F1Fo-ATP 合酶的表达产生了细胞内大部分的 ATP，据信它严格局限于线粒体，但最近在异位位置与氧化磷酸化（OXPHOS）的四个复合物或克雷布斯循环的酶一起被鉴定出来。这些蛋白质的鉴定主要通过蛋白质组学方法和质谱法完成——这些技术在增加我们对蛋白质组的理解方面具有巨大的潜力。ATP 合酶的异位存在归因于样品的污染或其作为表面受体的作用，显然与无关的配体结合，但 OXPHOS 蛋白有时被发现具有氧化磷酸化的催化活性，因为它们是被研究系统的真正组成部分。本文重点介绍了质谱法如何增加我们对亚细胞膜蛋白质组的理解。我们通过蛋白质组学研究回顾了最近关于 OXPHOS 线粒体外表达的证据，强调了通过结合这些数据我们可以学到什么。
