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Cryo-EM of native membranes reveals an intimate connection between the Krebs cycle and respiration in mycobacteria
Open accessPreprint — published as 10.1073/pnas.2423761122 · Paper page
Abstract
Imaging of endogenous protein complexes in their native membranes can reveal protein-protein interactions that are lost upon detergent solubilization. To investigate interactions in the mycobacterial oxidative phosphorylation machinery, we prepared inverted membrane vesicles from Mycobacterium smegmatis and enriched for vesicles containing complexes of interest by affinity chromatography. Electron cryomicroscopy (cryo-EM) of these vesicles revealed that malate-quinone oxidoreductase (Mqo), an enzyme from the Krebs cycle, physically associates with the electron transport chain Complex III 2 IV 2 (CIII 2 CIV 2 ) supercomplex. Analysis of the Mqo:CIII 2 CIV 2 interaction shows that CIII 2 CIV 2 is necessary for malate-driven, but not NADH- driven, electron transport chain activity and oxygen consumption. Further, the association of Mqo with CIII 2 CIV 2 enables electron transfer from malate to CIII 2 CIV 2 with millisecond kinetics. Together, these findings indicate a connection between the Krebs cycle and respiration that directs electrons along a single branch of the mycobacterial electron transport chain.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Di Trani, J. M., Yu, J., Courbon, G. M., Lobez Rodriguez, A. P., Cheung, C.-Y., Liang, Y., Coupland, C. E., Bueler, S. A., Cook, G. M., Brzezinski, P., & Rubinstein, J. L.
- Affiliations
- University of Toronto (CA)
- University of Otago (NZ)
- Great Ormond Street Hospital (GB)
- Queensland University of Technology (AU)
- Stockholm University (SE)
- Corresponding author
- Yu, Jiacheng
- Courbon, Gautier M.
- Cheung, Chen-Yi
- Brzezinski, Peter
- Rubinstein, John L.
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- openRxiv
- Published
- 2024-10-09
- Volume
- 122
- Issue
- 8
- Pages
- e2423761122-e2423761122
- ISSN
- 0027-8424 (ISSN-L)
- PMC
- PMC11874196
- OpenAlex
- W4407723076
- Cited by
- 16
- References
- 1
- Citations by year
- 2026: 12 · 2025: 3 · 2024: 1
- FWCI
- 3.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-nd
- www.biorxiv.org/about/FAQ#license (vor)
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Royal Society Te Apārangi
- Knut och Alice Wallenbergs Stiftelse (2019.0043)
- Canadian Institutes of Health Research (PJT162186)
- Marsden Fund
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- mycobacteria, TCA cycle, aerobic respiration, malate:quinone oxidoreductase, respiratory supercomplexes, cytochrome bc1 complex, cytochrome c oxidase, ATP synthase, electron transport chain, membrane vesicles, oxygen consumption
- MeSH terms
- Aerobiosis, Bacterial Proteins, Cell Membrane, Citric Acid Cycle, Electron Transport, Electron Transport Complex III, Mycobacterium smegmatis, Cryoelectron Microscopy
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