Difference between revisions of "Knapp-Wilson 2021 bioRxiv"
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{{Publication | {{Publication | ||
|title=Knapp-Wilson A, Pereira GC, Buzzard E, | |title=Knapp-Wilson A, Pereira GC, Buzzard E, Richardson A, Corey RA, Neal C, Verkade P, Halestrap AP, Gold VAM, Kuwabara P, Collinson I (2021) Maintenance of complex I and respiratory super-complexes by NDUF-11 is essential for respiratory function, mitochondrial structure and health in ''C. elegans''. bioRxiv doi: https://doi.org/10.1101/2021.01.06.425530. | ||
|info=[https://www.biorxiv.org/content/10.1101/2021.01.06.425530v1.full bioRxiv Open Access] | |info=[https://www.biorxiv.org/content/10.1101/2021.01.06.425530v1.full bioRxiv Open Access] | ||
|authors=Knapp-Wilson | |authors=Knapp-Wilson Amber, Pereira Goncalo C, Buzzard Emma, Richardson Andrew, Corey Robin A, Neal Chris, Verkade Paul, Halestrap Andrew P, Gold Vicki A M, Kuwabara Patricia, Collinson Ian | ||
|year=2021 | |year=2021 | ||
|journal=bioRxiv | |journal=bioRxiv | ||
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|keywords=Caenorhabditis elegans, Worm, Mitochondria, Respiration, Electron-transfer chain, Super-complexes, Respirasome, Mitochondrial ultrastructure, Cryo-electron tomography, NDUF-11 | |keywords=Caenorhabditis elegans, Worm, Mitochondria, Respiration, Electron-transfer chain, Super-complexes, Respirasome, Mitochondrial ultrastructure, Cryo-electron tomography, NDUF-11 | ||
|editor=[[Plangger M]] | |editor=[[Plangger M]] | ||
|mipnetlab=UK Bristol Halestrap AP | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|area=Respiration, mt-Structure;fission;fusion | |area=Respiration, mt-Structure;fission;fusion, Genetic knockout;overexpression | ||
|organism=Caenorhabditis elegans | |||
|preparations=Isolated mitochondria | |||
|enzymes=Supercomplex | |||
|couplingstates=LEAK, OXPHOS | |||
|pathways=N, S | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
|additional=2021-01 | |additional=2021-01 | ||
}} | }} |
Latest revision as of 18:07, 13 January 2021
Knapp-Wilson A, Pereira GC, Buzzard E, Richardson A, Corey RA, Neal C, Verkade P, Halestrap AP, Gold VAM, Kuwabara P, Collinson I (2021) Maintenance of complex I and respiratory super-complexes by NDUF-11 is essential for respiratory function, mitochondrial structure and health in C. elegans. bioRxiv doi: https://doi.org/10.1101/2021.01.06.425530. |
Knapp-Wilson Amber, Pereira Goncalo C, Buzzard Emma, Richardson Andrew, Corey Robin A, Neal Chris, Verkade Paul, Halestrap Andrew P, Gold Vicki A M, Kuwabara Patricia, Collinson Ian (2021) bioRxiv
Abstract: Mitochondrial super-complexes form around a conserved core of monomeric complex I and dimeric complex III; wherein subunit NDUFA11, of the former, is conspicuously situated at the interface. We identified B0491.5 (NDUF-11) as the C. elegans homologue, of which animals homozygous for a CRISPR-Cas9 generated knockout allele arrested at the L2 development stage. Reducing expression by RNAi allowed development to the adult stage, enabling characterisation of the consequences: destabilisation of complex I and its super-complexes, and perturbation of respiratory function. The loss of NADH-dehydrogenase activity is compensated by enhanced complex II activity, resulting in excessive detrimental ROS production. Meanwhile, electron cryo-tomography highlight aberrant cristae morphology and widening of the inter-membrane space and cristae junctions. The requirement of NDUF-11 for balanced respiration, mitochondrial morphology and development highlights the importance of complex I/ super-complex maintenance. Their perturbation by this, or other means, is likely to be the cause of metabolic stress and disease. β’ Keywords: Caenorhabditis elegans, Worm, Mitochondria, Respiration, Electron-transfer chain, Super-complexes, Respirasome, Mitochondrial ultrastructure, Cryo-electron tomography, NDUF-11 β’ Bioblast editor: Plangger M β’ O2k-Network Lab: UK Bristol Halestrap AP
Labels: MiParea: Respiration, mt-Structure;fission;fusion, Genetic knockout;overexpression
Organism: Caenorhabditis elegans
Preparation: Isolated mitochondria Enzyme: Supercomplex
Coupling state: LEAK, OXPHOS Pathway: N, S HRR: Oxygraph-2k
2021-01