| Respiratory chain complexes in dynamic mitochondria display a patchy distribution in life cells. | |
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MedLine Citation:
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PMID: 20689601 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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BACKGROUND: Mitochondria, the main suppliers of cellular energy, are dynamic organelles that fuse and divide frequently. Constraining these processes impairs mitochondrial is closely linked to certain neurodegenerative diseases. It is proposed that functional mitochondrial dynamics allows the exchange of compounds thereby providing a rescue mechanism. METHODOLOGY/PRINCIPAL FINDINGS: The question discussed in this paper is whether fusion and fission of mitochondria in different cell lines result in re-localization of respiratory chain (RC) complexes and of the ATP synthase. This was addressed by fusing cells containing mitochondria with respiratory complexes labelled with different fluorescent proteins and resolving their time dependent re-localization in living cells. We found a complete reshuffling of RC complexes throughout the entire chondriome in single HeLa cells within 2-3 h by organelle fusion and fission. Polykaryons of fused cells completely re-mixed their RC complexes in 10-24 h in a progressive way. In contrast to the recently described homogeneous mixing of matrix-targeted proteins or outer membrane proteins, the distribution of RC complexes and ATP synthase in fused hybrid mitochondria, however, was not homogeneous but patterned. Thus, complete equilibration of respiratory chain complexes as integral inner mitochondrial membrane complexes is a slow process compared with matrix proteins probably limited by complete fusion. In co-expressing cells, complex II is more homogenously distributed than complex I and V, resp. Indeed, this result argues for higher mobility and less integration in supercomplexes. CONCLUSION/SIGNIFICANCE: Our results clearly demonstrate that mitochondrial fusion and fission dynamics favours the re-mixing of all RC complexes within the chondriome. This permanent mixing avoids a static situation with a fixed composition of RC complexes per mitochondrion. |
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Authors:
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Britta Muster; Wladislaw Kohl; Ilka Wittig; Valentina Strecker; Friederike Joos; Winfried Haase; Jürgen Bereiter-Hahn; Karin Busch |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-07-30 |
Journal Detail:
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Title: PloS one Volume: 5 ISSN: 1932-6203 ISO Abbreviation: PLoS ONE Publication Date: 2010 |
Date Detail:
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Created Date: 2010-08-06 Completed Date: 2010-10-28 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101285081 Medline TA: PLoS One Country: United States |
Other Details:
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Languages: eng Pagination: e11910 Citation Subset: IM |
Affiliation:
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Institute of Kinematic Cell Research, Department of Biology, University of Frankfurt, Frankfurt/Main, Germany. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Electrophoresis Electrophoresis, Gel, Two-Dimensional Hela Cells Humans Membrane Fusion / physiology Microscopy, Electron Microscopy, Fluorescence Mitochondria / metabolism*, ultrastructure Mitochondrial Membranes / metabolism Mitochondrial Proton-Translocating ATPases / metabolism Oxygen Consumption |
| Chemical | |
Reg. No./Substance:
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EC 3.6.3.-/Mitochondrial Proton-Translocating ATPases |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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