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TitleAssembly of The Mitochondrial Complex I Assembly Complex Suggests a Regulatory Role for Deflavination.
Journal, issue, pagesAngew Chem Int Ed Engl, Vol. 60, Issue 9, Page 4689-4697, Year 2021
Publish dateFeb 23, 2021
AuthorsGabriele Giachin / Matthew Jessop / Romain Bouverot / Samira Acajjaoui / Melissa Saïdi / Anaïs Chretien / Maria Bacia-Verloop / Luca Signor / Philippe J Mas / Adrien Favier / Eve Borel Meneroud / Michael Hons / Darren J Hart / Eaazhisai Kandiah / Elisabetta Boeri Erba / Alain Buisson / Gordon Leonard / Irina Gutsche / Montserrat Soler-Lopez /
PubMed AbstractFatty acid β-oxidation (FAO) and oxidative phosphorylation (OXPHOS) are mitochondrial redox processes that generate ATP. The biogenesis of the respiratory Complex I, a 1 MDa multiprotein complex ...Fatty acid β-oxidation (FAO) and oxidative phosphorylation (OXPHOS) are mitochondrial redox processes that generate ATP. The biogenesis of the respiratory Complex I, a 1 MDa multiprotein complex that is responsible for initiating OXPHOS, is mediated by assembly factors including the mitochondrial complex I assembly (MCIA) complex. However, the organisation and the role of the MCIA complex are still unclear. Here we show that ECSIT functions as the bridging node of the MCIA core complex. Furthermore, cryo-electron microscopy together with biochemical and biophysical experiments reveal that the C-terminal domain of ECSIT directly binds to the vestigial dehydrogenase domain of the FAO enzyme ACAD9 and induces its deflavination, switching ACAD9 from its role in FAO to an MCIA factor. These findings provide the structural basis for the MCIA complex architecture and suggest a unique molecular mechanism for coordinating the regulation of the FAO and OXPHOS pathways to ensure an efficient energy production.
External linksAngew Chem Int Ed Engl / PubMed:33320993 / PubMed Central
MethodsEM (single particle)
Resolution7.8 Å
Structure data

EMDB-12055:
ACAD9-ECSIT-CTD (ACAD9 core)
Method: EM (single particle) / Resolution: 7.8 Å

Source
  • Homo sapiens (human)

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