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Architecture Mapping of the Inner Mitochondrial Membrane Proteome by Chemical Tools in Live Cells

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Title
Architecture Mapping of the Inner Mitochondrial Membrane Proteome by Chemical Tools in Live Cells
Author(s)
Lee S.-Y.; Kang M.-G.; Sanghee Shin; Kwak C.; Kwon T.; Seo J.K.; Jong-Seo Kim; Rhee H.-W.
Publication Date
2017-03
Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.139, no.10, pp.3651 - 3662
Publisher
AMER CHEMICAL SOC
Abstract
The inner mitochondrial membrane (IMM) proteome plays a central role in maintaining mitochondrial physiology and cellular metabolism. Various important biochemical reactions such as oxidative phosphorylation, metabolite production, and mitochondrial biogenesis are conducted by the IMM proteome, and mitochondria-targeted therapeutics have been developed for IMM proteins, which is deeply related for various human metabolic diseases including cancer and neurodegenerative diseases. However, the membrane topology of the IMM proteome remains largely unclear because of the lack of methods to evaluate it in live cells in a high-throughput manner. In this article, we reveal the in vivo topological direction of 135 IMM proteins, using an in situ-generated radical probe with genetically targeted peroxidase (APEX). Owing to the short lifetime of phenoxyl radicals generated in situ by submitochondrial targeted APEX and the impermeability of the IMM to small molecules, the solvent-exposed tyrosine residues of both the matrix and intermembrane space (IMS) sides of IMM proteins were exclusively labeled with the radical probe in live cells by Matrix-APEX and IMS-APEX, respectively and identified by mass spectrometry. From this analysis, we confirmed 58 IMM protein topologies and we could determine the topological direction of 77 IMM proteins whose topology at the IMM has not been fully characterized. We also found several IMM proteins (e.g., LETM1 and OXA1) whose topological information should be revised on the basis of our results. Overall, our identification of structural information on the mitochondrial inner-membrane proteome can provide valuable insights for the architecture and connectome of the IMM proteome in live cells. © 2017 American Chemical Society
URI
https://pr.ibs.re.kr/handle/8788114/3446
ISSN
0002-7863
Appears in Collections:
Center for RNA Research(RNA 연구단) > Journal Papers (저널논문)
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