Row-like organization of ATP synthase in intact mitochondria determined by cryo-electron tomography
| Autor: | Natalya V. Dudkina, Dagmar Lewejohann, Gert T. Oostergetel, Hans-Peter Braun, Egbert J. Boekema |
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| Přispěvatelé: | Electron Microscopy, Groningen Biomolecular Sciences and Biotechnology |
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Electron Microscope Tomography
TRANSMISSION Biophysics PROTEIN Mitochondrion Biochemistry INNER MEMBRANE RECONSTRUCTIONS ATP synthase gamma subunit Chlorophyta Organelle Image Processing Computer-Assisted Inner membrane DIMER ATP synthase biology Cell Membrane Cryoelectron Microscopy Polytomella Cell Biology biology.organism_classification SUBUNITS Cell biology Mitochondria ATP Synthetase Complexes STALK Electron tomography RESOLUTION biology.protein Cryo-electron tomography SUPRAMOLECULAR ORGANIZATION CRISTAE Dimerization |
| Zdroj: | Biochimica et Biophysica Acta-Bioenergetics, 1797(2), 272-277 |
| ISSN: | 0005-2728 |
| Popis: | The fine structure of intact, close-to-spherical mitochondria from the alga Polytomella was visualized by dual-axis cryo-electron tomography. The supramolecular organization of dimeric ATP synthase in the cristae membranes was investigated by averaging subvolumes of tomograms and 3D details at similar to 6 nm resolution were revealed. Oligomeric ATP synthase is composed of rows of dimers at 12 run intervals; the dimers make a slight angle along the row. In addition, the main features of monomeric ATP synthase, such as the conically shaped F, headpiece, central stalk and stator were revealed. This demonstrates the capability of dual-axis electron tomography to unravel details of proteins and their interactions in complete organelles. (C) 2009 Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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