Journal
STRUCTURE
Volume 29, Issue 9, Pages 1065-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2021.04.009
Keywords
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Funding
- European Research Council [StG-2012-311318]
- Agence Nationale de la Recherche [ANR-18-CE92-0032]
- Lundbeck Foundation BRAIN-STRUC initiative
- FRISBI within the Grenoble Partnership for Structural Biology (PSB) [ANR-10-INSB-05-02]
- GRAL within the Grenoble Partnership for Structural Biology (PSB) [ANR-10-LABX-49-01]
- Agence Nationale de la Recherche (ANR) [ANR-18-CE92-0032] Funding Source: Agence Nationale de la Recherche (ANR)
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The formation of TIM9.10 and TIM9.10.12 is related to a dynamic equilibrium among protein subunits and their large conformational dynamics, providing a new understanding of how mitochondria control the level of inter-membrane space chaperones.
Tim chaperones transport membrane proteins to the two mitochondrial membranes. TIM9.10, a 70 kDa protein complex formed by 3 copies of Tim9 and Tim10, guides its clients across the aqueous compartment. The TIM9.10.12 complex is the anchor point at the inner-membrane insertase TIM22. The subunit composition of TIM9.10.12 remains debated. Joint NMR, small-angle X-ray scattering, and MD simulation data allow us to derive a structural model of the TIM9.10.12 assembly, with a 2:3:1 stoichiometry (Tim9:Tim10:Tim12). Both TIM9.10 and TIM9.10.12 hexamers are in a dynamic equilibrium with their constituent subunits, exchanging on a minutes timescale. NMR data establish that the subunits exhibit large conformational dynamics: when the conserved cysteines of the CX3C-X-n-CX3C motifs are formed, short alpha helices are formed, and these are fully stabilized only upon formation of the mature hexameric chaperone. We propose that the continuous subunit exchange allows mitochondria to control their level of inter-membrane space chaperones.
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