Mitochondrial F-ATP Synthase Co-Migrating Proteins and Ca²⁺-Dependent Formation of Large Channels.

ABSTRACT: Monomers, dimers, and individual F_OF₁-ATP synthase subunits are, presumably, involved in the formation of the mitochondrial permeability transition pore (PTP), whose molecular structure, however, is still unknown. We hypothesized that, during the Ca²⁺-dependent assembly of a PTP complex, the F-ATP synthase (subunits) recruits mitochondrial proteins that do not interact or weakly interact with the F-ATP synthase under normal conditions. Therefore, we examined whether the PTP opening in mitochondria before the separation of supercomplexes via BN-PAGE will increase the channel stability and channel-forming capacity of isolated F-ATP synthase dimers and monomers in planar lipid membranes. Additionally, we studied the specific activity and the protein compositio

SUBMITTER: Nikiforova AB 

PROVIDER: S-EPMC10572550 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature